|
Name |
Accession |
Description |
Interval |
E-value |
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-598 |
0e+00 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 880.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 6 TRIAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVNLPSNLEKETTH 85
Cdd:COG1245 2 MRIAVVDRDRCQPKKCNYECIKYCPVNRTGKEAIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEDPVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 86 RYCANAFKLHRLPIPRPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFTKILEDDLK 165
Cdd:COG1245 82 RYGENGFRLYGLPVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKRFRGTELQDYFKKLANGEIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 166 AIIKPQYVDQIPKAAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:COG1245 162 VAHKPQYVDLIPKVFKGTVRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 246 YLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYVPTENLRFR 325
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEPGVYGVVSKPKSVRVGINQYLDGYLPEENVRIR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 326 DASLVFKVAETANEEEVKKMCmyKYPGMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVP 405
Cdd:COG1245 322 DEPIEFEVHAPRREKEEETLV--EYPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 406 VLNVSYKPQKISPKSTGSVRQLLHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLI 485
Cdd:COG1245 400 DLKISYKPQYISPDYDGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 486 DEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLSQLEIT 565
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASGPMDMREGMNRFLKELGIT 559
|
570 580 590
....*....|....*....|....*....|...
gi 108773782 566 FRRDPNNYRPRINKLNSIKDVEQKKSGNYFFLD 598
Cdd:COG1245 560 FRRDEETGRPRINKPGSYLDREQKERGEYYYYE 592
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-598 |
0e+00 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 859.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 6 TRIAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVNLPSNLEKETTH 85
Cdd:PRK13409 2 MRIAVVDYDRCQPKKCNYECIKYCPVVRTGEETIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEEPVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 86 RYCANAFKLHRLPIPRPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFTKILEDDLK 165
Cdd:PRK13409 82 RYGVNGFKLYGLPIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGTELQNYFKKLYNGEIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 166 AIIKPQYVDQIPKAAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:PRK13409 162 VVHKPQYVDLIPKVFKGKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 246 YLDVKQRLKAAITIRSLINpDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYVPTENLRFR 325
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAE-GKYVLVVEHDLAVLDYLADNVHIAYGEPGAYGVVSKPKGVRVGINEYLKGYLPEENMRIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 326 DASLVFKVAETANEEEVKKMCmyKYPGMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVP 405
Cdd:PRK13409 321 PEPIEFEERPPRDESERETLV--EYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 406 VLNVSYKPQKISPKSTGSVRQLLhEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLI 485
Cdd:PRK13409 399 ELKISYKPQYIKPDYDGTVEDLL-RSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 486 DEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLSQLEIT 565
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGKHGHASGPMDMREGMNRFLKELGIT 557
|
570 580 590
....*....|....*....|....*....|...
gi 108773782 566 FRRDPNNYRPRINKLNSIKDVEQKKSGNYFFLD 598
Cdd:PRK13409 558 FRRDEETGRPRVNKPGSYLDREQKERGEYYYAD 590
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-332 |
1.42e-170 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 484.56 E-value: 1.42e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 78 NLEKETTHRYCANAFKLHRLPIPRPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFT 157
Cdd:cd03236 1 ELEDEPVHRYGPNSFKLHRLPVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 158 KILEDDLKAIIKPQYVDQIPKAAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADI 237
Cdd:cd03236 81 KLLEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 238 FMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYV 317
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLDGYL 240
|
250
....*....|....*
gi 108773782 318 PTENLRFRDASLVFK 332
Cdd:cd03236 241 PTENMRFREESIEFE 255
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
348-592 |
2.25e-160 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 458.41 E-value: 2.25e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGG-EVPVLNVSYKPQKISPKSTGSVRQ 426
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDiEIELDTVSYKPQYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 LLHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKR 506
Cdd:cd03237 81 LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 507 FILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLSQLEITFRRDPNNYRPRINKLNSIKDV 586
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFLKNLDITFRRDPETGRPRINKLGSVKDR 240
|
....*.
gi 108773782 587 EQKKSG 592
Cdd:cd03237 241 EQKESG 246
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
349-567 |
4.80e-73 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 231.69 E-value: 4.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 349 KYPGMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGG-EVPVLNVSYKPQKISpkstgsvrql 427
Cdd:cd03222 2 LYPDCVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNdEWDGITPVYKPQYID---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 428 lhekirdaythpqfvtdvmkplqieniidqevqtLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRF 507
Cdd:cd03222 72 ----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 508 ILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLSQLEITFR 567
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITFR 177
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
101-313 |
5.44e-42 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 151.79 E-value: 5.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkydDPPDWQEILTYfrgselqnyftkileddlkaiiKPQYVdqIPKAa 180
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEG---DIEIELDTVSY----------------------KPQYI--KADY- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTVGSILDRKDETKT-----QAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKA 255
Cdd:cd03237 75 EGTVRDLLSSITKDFYthpyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 256 AITIRSLI-NPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFL 313
Cdd:cd03237 155 SKVIRRFAeNNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFL 213
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
79-321 |
2.99e-41 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 147.33 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 79 LEKETTHRYcANAFKLHRLPIPRPGEVLGLVGTNGIGKSTALKILAGKQKPNlgkyDDPPDWqeiltyfrgselqnyftk 158
Cdd:cd03222 2 LYPDCVKRY-GVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----GDNDEW------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 159 ileDDLKAIIKPQYVDqipkaakgtvgsildrkdetktqaivcqqldlthlkernvedLSGGELQRFACAVVCIQKADIF 238
Cdd:cd03222 59 ---DGITPVYKPQYID------------------------------------------LSGGELQRVAIAAALLRNATFY 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 239 MFDEPSSYLDVKQRLKAAITIRSLI-NPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYV 317
Cdd:cd03222 94 LFDEPSAYLDIEQRLNAARAIRRLSeEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYL 173
|
....
gi 108773782 318 PTEN 321
Cdd:cd03222 174 ITFR 177
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
371-560 |
3.96e-39 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 144.05 E-value: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 371 DSEIMVMLGENGTGKTTFIRMLAGRLKPDEG--GEVP----VLN--------------------VSYKPQKIS--PKS-T 421
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfDDPPdwdeILDefrgselqnyftkllegdvkVIVKPQYVDliPKAvK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 422 GSVRQLLHEKirdayTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAA 501
Cdd:cd03236 105 GKVGELLKKK-----DERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 502 RVVKRFILHaKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLS 560
Cdd:cd03236 180 RLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLD 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
101-534 |
2.21e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 125.02 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQkPNLGKYDDppdwqEILtyFRGSELQNYFTK--------ILEDDLKAIIKPQY 172
Cdd:COG1123 30 APGETVALVGESGSGKSTLALALMGLL-PHGGRISG-----EVL--LDGRDLLELSEAlrgrrigmVFQDPMTQLNPVTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VDQIPKAAKGTVGSildrKDETKTQAI-VCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQ 251
Cdd:COG1123 102 GDQIAEALENLGLS----RAEARARVLeLLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 252 RLKAAITIRSLI-NPDRYIIVVEHDLSVLDYLSDFICCLYGvpsayGVVTMPFSVREginIFLDGYVPTENLRFRDASLV 330
Cdd:COG1123 178 QAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDD-----GRIVEDGPPEE---ILAAPQALAAVPRLGAARGR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 331 FKVAETANEE--EVKKMCMYkYPGMKKKM-------------GEFeLAIVageftdseimvmlGENGTGKTTFIRMLAGR 395
Cdd:COG1123 250 AAPAAAAAEPllEVRNLSKR-YPVRGKGGvravddvsltlrrGET-LGLV-------------GESGSGKSTLARLLLGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 396 LKPDEGgevpvlNVSYKPQKISPKSTGSVRQLLHE----------------KIRDAYTHPQFVTDVMKPLQIENIIDQ-- 457
Cdd:COG1123 315 LRPTSG------SILFDGKDLTKLSRRSLRELRRRvqmvfqdpysslnprmTVGDIIAEPLRLHGLLSRAERRERVAEll 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 458 -EVQ-----------TLSGGELQRVALA--LCLgKPaDVYLIDEP-SAyLD-SEQrlmaARVVKRFI-LHAK--KTAFVV 518
Cdd:COG1123 389 eRVGlppdladryphELSGGQRQRVAIAraLAL-EP-KLLILDEPtSA-LDvSVQ----AQILNLLRdLQRElgLTYLFI 461
|
490
....*....|....*.
gi 108773782 519 EHDFIMATYLADRVIV 534
Cdd:COG1123 462 SHDLAVVRYIADRVAV 477
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
362-536 |
4.05e-27 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 109.09 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVL--NVSYKPQKISPKSTGSV-----RQLLHEKIRD 434
Cdd:cd03225 22 LTIKKGEFV-----LIVGPNGSGKSTLLRLLNGLLGPTSG-EVLVDgkDLTKLSLKELRRKVGLVfqnpdDQFFGPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 435 --AYTHPQF----------VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAAR 502
Cdd:cd03225 96 evAFGLENLglpeeeieerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 503 VVKRfiLHAK-KTAFVVEHDFIMATYLADRVIVFD 536
Cdd:cd03225 176 LLKK--LKAEgKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
101-276 |
8.71e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 104.44 E-value: 8.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyfrgselqnyftkILEDDLKAiikpqyvdqipkaa 180
Cdd:cd03214 23 EAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG---------EIL--------------LDGKDLAS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 kgtvgsiLDRKDETKTQAIVCQ---QLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAI 257
Cdd:cd03214 66 -------LSPKELARKIAYVPQaleLLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE 138
|
170 180
....*....|....*....|
gi 108773782 258 TIRSLIN-PDRYIIVVEHDL 276
Cdd:cd03214 139 LLRRLAReRGKTVVMVLHDL 158
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
362-536 |
1.34e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 103.09 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRQLLhekirdAYThPQf 441
Cdd:cd00267 20 LTLKAGEIV-----ALVGPNGSGKSTLLRAIAGLLKPTSG------EILIDGKDIAKLPLEELRRRI------GYV-PQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 442 vtdvmkplqieniidqevqtLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHaKKTAFVVEHD 521
Cdd:cd00267 81 --------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHD 139
|
170
....*....|....*
gi 108773782 522 FIMATYLADRVIVFD 536
Cdd:cd00267 140 PELAELAADRVIVLK 154
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
362-537 |
3.06e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 102.90 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDeGGEVPVLNVSYKpqKISPKStgsVRQLLhekirdAYThPQf 441
Cdd:cd03214 20 LSIEAGEIV-----GILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGKDLA--SLSPKE---LARKI------AYV-PQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 442 vtdVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD--SEQRLMaaRVVKRFILHAKKTAFVVE 519
Cdd:cd03214 81 ---ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiaHQIELL--ELLRRLARERGKTVVMVL 155
|
170
....*....|....*...
gi 108773782 520 HDFIMATYLADRVIVFDG 537
Cdd:cd03214 156 HDLNLAARYADRVILLKD 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
362-537 |
1.29e-24 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 103.20 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLN---------VSYKPQKISPKSTGSVRQLL 428
Cdd:COG1120 22 LSLPPGEVT-----ALLGPNGSGKSTLLRALAGLLKPSSGevllDGRDLASlsrrelarrIAYVPQEPPAPFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 429 ------HEKIRDAYTH--PQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD--SEQRL 498
Cdd:COG1120 97 algrypHLGLFGRPSAedREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDlaHQLEV 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 108773782 499 MaaRVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDG 537
Cdd:COG1120 177 L--ELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
368-536 |
7.37e-24 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 100.70 E-value: 7.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVPVLNVSYKPQKIS--PKSTG-----SVRQ------LLH 429
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGsilidGEDVRKEPREARRQIGvlPDERGlydrlTVREniryfaELY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 430 EKIRDAYthPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDseqrLMAARVVKRFIL 509
Cdd:COG4555 103 GLFDEEL--KKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD----VMARRLLREILR 176
|
170 180 190
....*....|....*....|....*....|
gi 108773782 510 HAK---KTAFVVEHDFIMATYLADRVIVFD 536
Cdd:COG4555 177 ALKkegKTVLFSSHIMQEVEALCDRVVILH 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
348-537 |
1.85e-23 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 99.33 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVR-- 425
Cdd:COG1122 8 FSYPGGTPALDDVSLSIEKGEFV-----AIIGPNGSGKSTLLRLLNGLLKPTSG------EVLVDGKDITKKNLRELRrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 426 ----------QLL------------------HEKIRDAythpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALA--LC 475
Cdd:COG1122 77 vglvfqnpddQLFaptveedvafgpenlglpREEIRER------VEEALELVGLEHLADRPPHELSGGQKQRVAIAgvLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108773782 476 LgKPaDVYLIDEPSAYLDSEQRLMAARVVKRfiLHAKKTAFV-VEHDFIMATYLADRVIVFDG 537
Cdd:COG1122 151 M-EP-EVLVLDEPTAGLDPRGRRELLELLKR--LNKEGKTVIiVTHDLDLVAELADRVIVLDD 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
101-289 |
3.28e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 97.92 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDDPPDWQEILTYFR---GSELQN----YFTKILEDDLkaiikpq 171
Cdd:cd03225 25 KKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlVDGKDLTKLSLKELRrkvGLVFQNpddqFFGPTVEEEV------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 172 yvdqipkaAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQ 251
Cdd:cd03225 98 --------AFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 108773782 252 RLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCL 289
Cdd:cd03225 170 RRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
101-276 |
4.87e-23 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 98.58 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyfrgselqnyftkILEDDLKAIiKPQ-------YV 173
Cdd:COG1120 25 PPGEVTALLGPNGSGKSTLLRALAGLLKPSSG---------EVL--------------LDGRDLASL-SRRelarriaYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 174 DQIPKAAKG-TV--------------GSILDRKDETK-TQAIvcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADI 237
Cdd:COG1120 81 PQEPPAPFGlTVrelvalgryphlglFGRPSAEDREAvEEAL--ERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 238 FMFDEPSSYLDVKQRLKAAITIRSLINP-DRYIIVVEHDL 276
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDL 198
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
102-536 |
9.98e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 9.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDW------QEILTYFRGSELQNYFT------KILEDDLKAIIK 169
Cdd:COG0488 23 PGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigylpQEPPLDDDLTVLDTVLDgdaelrALEAELEELEAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 170 PQYVDQIPKAAkGTVGSILDRKD----ETKTQAIvCQQLDLTHLK-ERNVEDLSGGELQRFACAVVCIQKADIFMFDEPS 244
Cdd:COG0488 103 LAEPDEDLERL-AELQEEFEALGgweaEARAEEI-LSGLGFPEEDlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 245 SYLDVK------QRLKaaitirslinpdRY---IIVVEHDLSVLDylsdficclygvpsayGVVTMPFSV-REGINIFLD 314
Cdd:COG0488 181 NHLDLEsiewleEFLK------------NYpgtVLVVSHDRYFLD----------------RVATRILELdRGKLTLYPG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 315 GYvpTENLRFRDASLvfKVAETANEEEVKKM---------CMYKYPGMKK---------KM---------GEFELAIVAG 367
Cdd:COG0488 233 NY--SAYLEQRAERL--EQEAAAYAKQQKKIakeeefirrFRAKARKAKQaqsrikaleKLereepprrdKTVEIRFPPP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 E---------------------FTDSEIMVM-------LGENGTGKTTFIRMLAGRLKPDEgGEV---PVLNVSYKPQKi 416
Cdd:COG0488 309 ErlgkkvleleglsksygdktlLDDLSLRIDrgdriglIGPNGAGKSTLLKLLAGELEPDS-GTVklgETVKIGYFDQH- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 417 spkstgsvRQLLHEK------IRDAYT--HPQFV-----------TDVMKPlqieniidqeVQTLSGGELQRVALALCLG 477
Cdd:COG0488 387 --------QEELDPDktvldeLRDGAPggTEQEVrgylgrflfsgDDAFKP----------VGVLSGGEKARLALAKLLL 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 478 KPADVYLIDEPSAYLDSEQRlmaaRVVKRFILHAKKTAFVVEHD--FIMAtyLADRVIVFD 536
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETL----EALEEALDDFPGTVLLVSHDryFLDR--VATRILEFE 503
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
352-535 |
1.44e-22 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 96.64 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 352 GMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPD------EGGEVPVL-----NVSYKPQKIS--P 418
Cdd:cd03299 5 NLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsgkillNGKDITNLppekrDISYVPQNYAlfP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 419 KST------GSVRQLLHEKIRDaythPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYL 492
Cdd:cd03299 85 HMTvykniaYGLKKRKVDKKEI----ERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 108773782 493 DSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVF 535
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
362-537 |
1.56e-22 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 96.06 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVPVL---NVSYKPQK--ISPKSTGSVRQLL--- 428
Cdd:cd03235 20 FEVKPGEFL-----AIVGPNGAGKSTLLKAILGLLKPTSGsirvfGKPLEKerkRIGYVPQRrsIDRDFPISVRDVVlmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 429 ---HEKIRDAYTHPQF--VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARV 503
Cdd:cd03235 95 lygHKGLFRRLSKADKakVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYEL 174
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 504 VKRfiLHAK-KTAFVVEHDFIMATYLADRVIVFDG 537
Cdd:cd03235 175 LRE--LRREgMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
348-536 |
1.61e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 96.17 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKKMGEFELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSYKPQKIspkstGS 423
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEF-----VVLLGPSGCGKTTTLRMIAGLEEPTSGriyiGGRDVTDLPPKDRDI-----AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 424 VRQLL----HEKIRDAYTHP------------QFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDE 487
Cdd:cd03301 77 VFQNYalypHMTVYDNIAFGlklrkvpkdeidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 488 PSAYLDSEQRL-MAARVVKrfiLHAK-KTAFV-VEHDFIMATYLADRVIVFD 536
Cdd:cd03301 157 PLSNLDAKLRVqMRAELKR---LQQRlGTTTIyVTHDQVEAMTMADRIAVMN 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
373-537 |
2.44e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.90 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVL-------------NVSYKPQKISPKSTGSVRQLL--HEKIR--DA 435
Cdd:COG1131 27 EIFGLLGPNGAGKTTTIRMLLGLLRPTSG-EVRVLgedvardpaevrrRIGYVPQEPALYPDLTVRENLrfFARLYglPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 436 YTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRlmaaRVVKRFILHAK--- 512
Cdd:COG1131 106 KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEAR----RELWELLRELAaeg 181
|
170 180
....*....|....*....|....*..
gi 108773782 513 KTAFVVEHdfIM--ATYLADRVIVFDG 537
Cdd:COG1131 182 KTVLLSTH--YLeeAERLCDRVAIIDK 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
362-537 |
6.56e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 95.16 E-value: 6.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVPVLN---VSYKPQKIS-----PkstGSVRQL- 427
Cdd:COG1121 27 LTIPPGEFV-----AIVGPNGAGKSTLLKAILGLLPPTSGtvrlfGKPPRRArrrIGYVPQRAEvdwdfP---ITVRDVv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 428 -------------LHEKIRDAythpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD- 493
Cdd:COG1121 99 lmgrygrrglfrrPSRADREA------VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDa 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 108773782 494 -SEQRLMaaRVVKRfiLHAK-KTAFVVEHDFIMATYLADRVIVFDG 537
Cdd:COG1121 173 aTEEALY--ELLRE--LRREgKTILVVTHDLGAVREYFDRVLLLNR 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
358-534 |
3.53e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.80 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 358 GEFELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLN---------VSYKPQKispkST--- 421
Cdd:COG4619 17 SPVSLTLEAGEC-----VAITGPSGSGKSTLLRALADLDPPTSGeiylDGKPLSAmpppewrrqVAYVPQE----PAlwg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 422 GSVRQLLHE--KIRDAYTHPQFVTDVMKPLQI-ENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRL 498
Cdd:COG4619 88 GTVRDNLPFpfQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 108773782 499 MAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIV 534
Cdd:COG4619 168 RVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
373-534 |
9.81e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 89.76 E-value: 9.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSYKPQKISPKS-TGSVRQllhekirdaytHPQFVTDvMKPlqI 451
Cdd:cd03230 27 EIYGLLGPNGAGKTTLIKIILGLLKPDSG-EIKVLGKDIKKEPEEVKRrIGYLPE-----------EPSLYEN-LTV--R 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 452 ENIidqevqTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRlmaaRVVKRFILHAK---KTAFVVEHDFIMATYL 528
Cdd:cd03230 92 ENL------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR----REFWELLRELKkegKTILLSSHILEEAERL 161
|
....*.
gi 108773782 529 ADRVIV 534
Cdd:cd03230 162 CDRVAI 167
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
352-536 |
2.87e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 88.40 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 352 GMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISpkSTGSVRQLLHEK 431
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIV-----ALLGPSGSGKSTLLRCIAGLEEPDSG------SILIDGEDLT--DLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 432 IRDAYTHPQFVT--DVMkplqiENIidqeVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRfiL 509
Cdd:cd03229 78 IGMVFQDFALFPhlTVL-----ENI----ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKS--L 146
|
170 180
....*....|....*....|....*....
gi 108773782 510 HAK--KTAFVVEHDFIMATYLADRVIVFD 536
Cdd:cd03229 147 QAQlgITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
360-534 |
3.48e-20 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 89.12 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 360 FELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSykPQKispKSTGSVRQ---L----- 427
Cdd:cd03259 19 LSLTVEPGEFL-----ALLGPSGCGKTTLLRLIAGLERPDSGeiliDGRDVTGVP--PER---RNIGMVFQdyaLfphlt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 428 --------LHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLM 499
Cdd:cd03259 89 vaeniafgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREE 168
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 500 AARVVKRFILHAKKTAFVVEHDFIMATYLADRVIV 534
Cdd:cd03259 169 LREELKELQRELGITTIYVTHDQEEALALADRIAV 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
102-287 |
8.49e-20 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 87.97 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDdppdwqeiltyfrgselqnYFTKILEDDLKAIikpQYVDQI----- 176
Cdd:cd03235 24 PGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR-------------------VFGKPLEKERKRI---GYVPQRrsidr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 177 --PKAAKGTVGS----------ILDRKDETK-TQAIvcQQLDLTHLKERNVEDLSGGELQR--FACAVVciQKADIFMFD 241
Cdd:cd03235 82 dfPISVRDVVLMglyghkglfrRLSKADKAKvDEAL--ERVGLSELADRQIGELSGGQQQRvlLARALV--QDPDLLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 108773782 242 EPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDL-SVLDYLSDFIC 287
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLL 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
101-289 |
1.32e-19 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 85.76 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYddppdwqeiltYFRGSELQNYFTKILEDDLkaiikpQYVDQipkaa 180
Cdd:cd00267 23 KAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI-----------LIDGKDIAKLPLEELRRRI------GYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 kgtvgsildrkdetktqaivcqqldlthlkernvedLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIR 260
Cdd:cd00267 81 ------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180
....*....|....*....|....*....
gi 108773782 261 SLINPDRYIIVVEHDLSVLDYLSDFICCL 289
Cdd:cd00267 125 ELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
373-490 |
5.18e-19 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 83.85 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG-----------GEVPVL--NVSYKPQKISPKSTGSVRQLLHEKIRDAYTHP 439
Cdd:pfam00005 12 EILALVGPNGAGKSTLLKLIAGLLSPTEGtilldgqdltdDERKSLrkEIGYVFQDPQLFPRLTVRENLRLGLLLKGLSK 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 440 ----QFVTDVMKPLQIENIIDQEVQ----TLSGGELQRVALALCLGKPADVYLIDEPSA 490
Cdd:pfam00005 92 rekdARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
101-286 |
6.21e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 85.39 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDDPPDWQEILTYFRGSELQN----YFTKILEDDLkaiikpqyvd 174
Cdd:cd03226 24 YAGEIIALTGKNGAGKTTLAKILAGLIKESSGSilLNGKPIKAKERRKSIGYVMQDvdyqLFTDSVREEL---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 qipkaakgTVGSILDRKDETKTQAIVcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLK 254
Cdd:cd03226 94 --------LLGLKELDAGNEQAETVL-KDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 255 AAITIRSLINPDRYIIVVEHDLSVLDYLSDFI 286
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
348-537 |
8.14e-19 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 83.97 E-value: 8.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKK-MGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSYKpqKISPKStgsvrq 426
Cdd:cd03228 8 FSYPGRPKPvLKDVSLTIKPGEKV-----AIVGPSGSGKSTLLKLLLRLYDPTSG-EILIDGVDLR--DLDLES------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 lLHEKIrdAYThPQ----FVTDVMkplqiENIidqevqtLSGGELQRVALALCLGKPADVYLIDEPSAYLD--SEQRLMA 500
Cdd:cd03228 74 -LRKNI--AYV-PQdpflFSGTIR-----ENI-------LSGGQRQRIAIARALLRDPPILILDEATSALDpeTEALILE 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 108773782 501 ArvVKRfiLHAKKTAFVVEHDFIMATyLADRVIVFDG 537
Cdd:cd03228 138 A--LRA--LAKGKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
371-534 |
8.38e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 85.50 E-value: 8.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 371 DSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-GEVPVLNVSYKPQK------ISPKSTG-----SVRQL------LHEKI 432
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGfATVDGFDVVKEPAEarrrlgFVSDSTGlydrlTARENleyfagLYGLK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 433 RDAYThpQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDseqrLMAARVVKRFILHAK 512
Cdd:cd03266 110 GDELT--ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD----VMATRALREFIRQLR 183
|
170 180
....*....|....*....|....*
gi 108773782 513 ---KTAFVVEHDFIMATYLADRVIV 534
Cdd:cd03266 184 algKCILFSTHIMQEVERLCDRVVV 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
348-537 |
1.59e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 89.05 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLN---------VSYKPQ 414
Cdd:COG4988 344 FSYPGGRPALDGLSLTIPPGERV-----ALVGPSGAGKSTLLNLLLGFLPPYSGsiliNGVDLSDldpaswrrqIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 415 K--ISPkstGSVR------------QLLHEKIRDAYTHpQFVTDVmkPLQIENIIDQEVQTLSGGELQRVALALCLGKPA 480
Cdd:COG4988 419 NpyLFA---GTIRenlrlgrpdasdEELEAALEAAGLD-EFVAAL--PDGLDTPLGEGGRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 481 DVYLIDEPSAYLD--SEQRLMAArvVKRfiLHAKKTAFVVEHDfIMATYLADRVIVFDG 537
Cdd:COG4988 493 PLLLLDEPTAHLDaeTEAEILQA--LRR--LAKGRTVILITHR-LALLAQADRILVLDD 546
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
103-532 |
2.35e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.32 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAG--KQKPNLGK------------YDDPPD--------------------WQEILTYFR 148
Cdd:TIGR03269 26 GEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRiiyhvalcekcgYVERPSkvgepcpvcggtlepeevdfWNLSDKLRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 149 GSE------LQNYFT-----KILEDDLKAIikpqyvDQIPKAAKGTVGSILDRKDETKtqaivcqqldLTHLKERNVEDL 217
Cdd:TIGR03269 106 RIRkriaimLQRTFAlygddTVLDNVLEAL------EEIGYEGKEAVGRAVDLIEMVQ----------LSHRITHIARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 218 SGGELQRFACAVVCIQKADIFMFDEPSSYLD------VKQRLKAAItirslINPDRYIIVVEHDLSVLDYLSDficclYG 291
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtaklVHNALEEAV-----KASGISMVLTSHWPEVIEDLSD-----KA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 292 VPSAYGVVTMPFSVREGINIFLDGYVPTENlrfrdaslvFKVAETANE----EEVKKMCMYKYPGMKKKMGEFELAIVAG 367
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVAVFMEGVSEVEK---------ECEVEVGEPiikvRNVSKRYISVDRGVVKAVDNVSLEVKEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EftdseIMVMLGENGTGKTTFIRMLAGRLKPDEGG-EVPVLNVSYKPQKISPKSTGSVRQ---LLHEKIrDAYTHPQFVT 443
Cdd:TIGR03269 311 E-----IFGIVGTSGAGKTTLSKIIAGVLEPTSGEvNVRVGDEWVDMTKPGPDGRGRAKRyigILHQEY-DLYPHRTVLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 444 DVMKPLQIE-------------------------NIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRl 498
Cdd:TIGR03269 385 NLTEAIGLElpdelarmkavitlkmvgfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITK- 463
|
490 500 510
....*....|....*....|....*....|....*...
gi 108773782 499 maaRVVKRFILHAKK----TAFVVEHDFIMATYLADRV 532
Cdd:TIGR03269 464 ---VDVTHSILKAREemeqTFIIVSHDMDFVLDVCDRA 498
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
362-533 |
2.77e-18 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 83.46 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPdEGGEVpVLNVSYKPQKISPKSTG-------------SVRQLL 428
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-SSGSI-LLNGKPIKAKERRKSIGyvmqdvdyqlftdSVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 429 HEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALA--LCLGKpaDVYLIDEPSAYLDSEQRLMAARVVKR 506
Cdd:cd03226 94 LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAaaLLSGK--DLLIFDEPTSGLDYKNMERVGELIRE 171
|
170 180
....*....|....*....|....*..
gi 108773782 507 fILHAKKTAFVVEHDFIMATYLADRVI 533
Cdd:cd03226 172 -LAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
101-287 |
2.96e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 84.37 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyfrgselqnYFTKILEDDLKAIikpQYVDQIPKAA 180
Cdd:COG1121 30 PPGEFVAIVGPNGAGKSTLLKAILGLLPPTSG---------TVR----------LFGKPPRRARRRI---GYVPQRAEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KG---TV--------------GSILDRKDETKTQAIVcQQLDLTHLKERNVEDLSGGELQR--FACAVVciQKADIFMFD 241
Cdd:COG1121 88 WDfpiTVrdvvlmgrygrrglFRRPSRADREAVDEAL-ERVGLEDLADRPIGELSGGQQQRvlLARALA--QDPDLLLLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 108773782 242 EPSSYLDVKQRlkAAI--TIRSLINPDRYIIVVEHDLS-VLDYLSDFIC 287
Cdd:COG1121 165 EPFAGVDAATE--EALyeLLRELRREGKTILVVTHDLGaVREYFDRVLL 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
101-284 |
4.04e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 84.08 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEIltYFRGSELQNYFTKiledDLKAIIkpQYVDQIPKAA 180
Cdd:COG1124 29 APGESFGLVGESGSGKSTLLRALAGLERPWSG---------EV--TFDGRPVTRRRRK----AFRRRV--QMVFQDPYAS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 ---KGTVGSILD------RKDETKTQAI-VCQQLDLT-HLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:COG1124 92 lhpRHTVDRILAeplrihGLPDREERIAeLLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 108773782 250 K---------QRLKAA--ITirslinpdryIIVVEHDLSVLDYLSD 284
Cdd:COG1124 172 SvqaeilnllKDLREErgLT----------YLFVSHDLAVVAHLCD 207
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
362-541 |
5.54e-18 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 82.90 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVpvlNVSYKPQKISPKSTGSVRQ---LL-HEKIRDayt 437
Cdd:cd03293 25 LSVEEGEFV-----ALVGPSGCGKSTLLRIIAGLERPTSG-EV---LVDGEPVTGPGPDRGYVFQqdaLLpWLTVLD--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 438 hpqfvtDVMKPLQIENIIDQEVQT---------------------LSGGELQRVALALCL-GKPaDVYLIDEPSAYLDSE 495
Cdd:cd03293 93 ------NVALGLELQGVPKAEAREraeellelvglsgfenayphqLSGGMRQRVALARALaVDP-DVLLLDEPFSALDAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 108773782 496 QRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSK 541
Cdd:cd03293 166 TREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGR 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
101-284 |
8.31e-18 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 82.98 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YD------DPPDWQEILTYFRGselQNYFTKIL--EDDLKAIIkp 170
Cdd:COG4555 25 KDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilIDgedvrkEPREARRQIGVLPD---ERGLYDRLtvRENIRYFA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 171 qyvdqipkAAKGtvgsILDRKDETKTQAIVcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:COG4555 100 --------ELYG----LFDEELKKRIEELI-ELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 251 QRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSD 284
Cdd:COG4555 167 ARRLLREILRALKKEGKTVLFSSHIMQEVEALCD 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
362-538 |
1.02e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 84.74 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSykPQK--IS---------PksTGSVRQ 426
Cdd:COG3839 24 LDIEDGEF-----LVLLGPSGCGKSTLLRMIAGLEDPTSGeiliGGRDVTDLP--PKDrnIAmvfqsyalyP--HMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 -----LLHEKIRDAYTHPQfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAA 501
Cdd:COG3839 95 niafpLKLRKVPKAEIDRR-VREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 502 RVVKRfiLHAK-KTAFV-VEHDFIMATYLADRVIVF-DGV 538
Cdd:COG3839 174 AEIKR--LHRRlGTTTIyVTHDQVEAMTLADRIAVMnDGR 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
97-276 |
1.30e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 97 LPIPrPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDDPPDWQeiltyFRGSELQNYFTkileddlkaiikpqYVD 174
Cdd:PRK11231 23 LSLP-TGKITALIGPNGCGKSTLLKCFARLLTPQSGTvfLGDKPISM-----LSSRQLARRLA--------------LLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 QIPKAAKG-TVGSI--------------LDRKDETK-TQAIvcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIF 238
Cdd:PRK11231 83 QHHLTPEGiTVRELvaygrspwlslwgrLSAEDNARvNQAM--EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 108773782 239 MFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDL 276
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDL 198
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
355-537 |
1.66e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 81.57 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 355 KKMGEFELAIvagEFT-DSEIMVMLGENGTGKTTFIRMLAGRLKPDeGGEV----PVLNVSYKPQKISPKSTG------- 422
Cdd:cd03297 8 KRLPDFTLKI---DFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPD-GGTIvlngTVLFDSRKKINLPPQQRKiglvfqq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 423 -------SVRQLLHEKIRDAYTHP--QFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD 493
Cdd:cd03297 84 yalfphlNVRENLAFGLKRKRNREdrISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 108773782 494 SEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVF-DG 537
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMeDG 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
101-291 |
2.83e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 81.01 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYddppdwqeiltYFRGSELQNYFTKILEDDLKAIikpQYVDQIPKAA 180
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILGLLKPTSGSI-----------IFDGKDLLKLSRRLRKIRRKEI---QMVFQDPMSS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 ---KGTVGSIL--------DRKDETKTQAIVCQQLDLTHLKERnVED-----LSGGELQRFACAVVCIQKADIFMFDEPS 244
Cdd:cd03257 95 lnpRMTIGEQIaeplrihgKLSKKEARKEAVLLLLVGVGLPEE-VLNrypheLSGGQRQRVAIARALALNPKLLIADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 245 SYLDVKqrLKAAI--TIRSLInpDRY---IIVVEHDLSVLDYLSDFICCLYG 291
Cdd:cd03257 174 SALDVS--VQAQIldLLKKLQ--EELgltLLFITHDLGVVAKIADRVAVMYA 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
101-284 |
4.34e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 80.88 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--------YDDPPDWQEILTYFrgseLQNYFtkiLEDDLKAIikpQY 172
Cdd:COG1131 24 EPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgedvARDPAEVRRRIGYV----PQEPA---LYPDLTVR---EN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VDqipkaakgTVGSILDRKDETKTQAI--VCQQLDLTHLKERNVEDLSGGELQR--FACAVVCiqKADIFMFDEPSSYLD 248
Cdd:COG1131 94 LR--------FFARLYGLPRKEARERIdeLLELFGLTDAADRKVGTLSGGMKQRlgLALALLH--DPELLILDEPTSGLD 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 108773782 249 VKQR--LKAAitIRSLINPDRYIIVVEHDLSVLDYLSD 284
Cdd:COG1131 164 PEARreLWEL--LRELAAEGKTVLLSTHYLEEAERLCD 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
362-537 |
6.02e-17 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 79.84 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNV---SYKPQKISP---KSTGSVRQ--------- 426
Cdd:cd03255 25 LSIEKGEFV-----AIVGPSGSGKSTLLNILGGLDRPTSG-EVRVDGTdisKLSEKELAAfrrRHIGFVFQsfnllpdlt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 --------LLHEKIRDAYTHPQfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRL 498
Cdd:cd03255 99 alenvelpLLLAGVPKKERRER-AEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 499 MAARVVKRFILHAKKTAFVVEHDFIMATYlADRVIVF-DG 537
Cdd:cd03255 178 EVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELrDG 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
373-521 |
9.34e-17 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 79.06 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVPVL-------NVSYKPQKISPKSTGSVRQLL--HEKIRDAYTH 438
Cdd:COG4133 29 EALALTGPNGSGKTTLLRILAGLLPPSAGevlwnGEPIRDaredyrrRLAYLGHADGLKPELTVRENLrfWAALYGLRAD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 439 PQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFiLHAKKTAFVV 518
Cdd:COG4133 109 REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLT 187
|
...
gi 108773782 519 EHD 521
Cdd:COG4133 188 THQ 190
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
378-537 |
1.46e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 79.46 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 378 LGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRQllheKIR----DAYT--HPQF-VTDVMK-PL 449
Cdd:COG1124 37 VGESGSGKSTLLRALAGLERPWSG------EVTFDGRPVTRRRRKAFRR----RVQmvfqDPYAslHPRHtVDRILAePL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 450 QIENIIDQEVQT--------------------LSGGELQRVAL--ALCLgKPaDVYLIDEPSAYLD-SEQRLMaARVVKR 506
Cdd:COG1124 107 RIHGLPDREERIaelleqvglppsfldryphqLSGGQRQRVAIarALIL-EP-ELLLLDEPTSALDvSVQAEI-LNLLKD 183
|
170 180 190
....*....|....*....|....*....|.
gi 108773782 507 FILHAKKTAFVVEHDFIMATYLADRVIVFDG 537
Cdd:COG1124 184 LREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
373-537 |
1.63e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 76.72 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlnvsyKPQKISPKSTGSVRQLlhekirdaythpqfvtdvmkplqie 452
Cdd:cd03221 27 DRIGLVGRNGAGKSTLLKLIAGELEPDEG----------IVTWGSTVKIGYFEQL------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 453 niidqevqtlSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFilhaKKTAFVVEHDFIMATYLADRV 532
Cdd:cd03221 72 ----------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY----PGTVILVSHDRYFLDQVATKI 137
|
....*
gi 108773782 533 IVFDG 537
Cdd:cd03221 138 IELED 142
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
101-290 |
2.09e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 82.26 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELqnyfTKILEDDLKAIIKP-QYVDQIPKA 179
Cdd:COG1123 289 RRGETLGLVGESGSGKSTLARLLLGLLRPTSG---------SIL--FDGKDL----TKLSRRSLRELRRRvQMVFQDPYS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 180 A---KGTVGSILDR-------KDETKTQAIVCQQLDLTHL----KERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:COG1123 354 SlnpRMTVGDIIAEplrlhglLSRAERRERVAELLERVGLppdlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTS 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 108773782 246 YLDVKQRlkAAI--TIRSLinPDRY---IIVVEHDLSVLDYLSDFICCLY 290
Cdd:COG1123 434 ALDVSVQ--AQIlnLLRDL--QRELgltYLFISHDLAVVRYIADRVAVMY 479
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
362-535 |
3.28e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.27 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG--GEVPVLNVSYKPQKISPKST-----------------G 422
Cdd:NF040873 13 LTIPAGSLT-----AVVGPNGSGKSTLLKVLAGVLRPTSGtvRRAGGARVAYVPQRSEVPDSlpltvrdlvamgrwarrG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 423 SVRQLLHEKIRDaythpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAAR 502
Cdd:NF040873 88 LWRRLTRDDRAA-------VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 503 VVKRfiLHAKKTAFV-VEHDFIMATyLADRVIVF 535
Cdd:NF040873 161 LLAE--EHARGATVVvVTHDLELVR-RADPCVLL 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
373-536 |
3.99e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 77.86 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG-----G---------EVPVLNVSYKPQKISPKSTGSVRQ------------ 426
Cdd:cd03219 27 EIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlfdGeditglpphEIARLGIGRTFQIPRLFPELTVLEnvmvaaqartgs 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 --LLHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVV 504
Cdd:cd03219 107 glLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELI 186
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 505 KRfiLHAKKTAFV-VEHD--FIMAtyLADRVIVFD 536
Cdd:cd03219 187 RE--LRERGITVLlVEHDmdVVMS--LADRVTVLD 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
101-289 |
4.69e-16 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 77.76 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDDPPDWQEILTYFR---GSELQNY----FTKILEDD----LKAI 167
Cdd:COG1122 25 EKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlVDGKDITKKNLRELRrkvGLVFQNPddqlFAPTVEEDvafgPENL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 168 ikpqyvdQIPKAAkgtvgsILDRKDEtktqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYL 247
Cdd:COG1122 105 -------GLPREE------IRERVEE------ALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 108773782 248 DVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCL 289
Cdd:COG1122 166 DPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVL 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
348-537 |
5.37e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 77.24 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKKmgefELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSYK---PQKISpKSTGSV 424
Cdd:cd03245 10 FSYPNQEIP----ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSG-SVLLDGTDIRqldPADLR-RNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 425 RQ---LLHEKIRD--AYTHPqFVTD--VMKPLQIENI----------IDQEV----QTLSGGELQRVALA-LCLGKPAdV 482
Cdd:cd03245 84 PQdvtLFYGTLRDniTLGAP-LADDerILRAAELAGVtdfvnkhpngLDLQIgergRGLSGGQRQAVALArALLNDPP-I 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 483 YLIDEPSAYLD--SEQRLMAArvVKRFILHakKTAFVVEHDFIMATyLADRVIVFDG 537
Cdd:cd03245 162 LLLDEPTSAMDmnSEERLKER--LRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDS 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
350-540 |
5.99e-16 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 77.61 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 350 YPGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRQL-- 427
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEFV-----ALIGPSGAGKSTLLRCLNGLVEPTSG------SVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 428 ----------LHEKI---------RDAYTHP-----QFVTDVMKPLQIE-----NIID---QEVQTLSGGELQRVALALC 475
Cdd:cd03256 79 qigmifqqfnLIERLsvlenvlsgRLGRRSTwrslfGLFPKEEKQRALAalervGLLDkayQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 476 LGKPADVYLIDEPSAYLD--SEQRLMaaRVVKRFILHAKKTAFVVEHDFIMATYLADRV-------IVFDGVPS 540
Cdd:cd03256 159 LMQQPKLILADEPVASLDpaSSRQVM--DLLKRINREEGITVIVSLHQVDLAREYADRIvglkdgrIVFDGPPA 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
341-537 |
6.64e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.11 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 341 EVKKMCmYKYPGMKKkmgeFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGG------EVPVLNVSYKPQ 414
Cdd:PRK13632 9 KVENVS-FSYPNSEN----NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEikidgiTISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 415 KI-----SPKS--TGSV-----------RQLLHEKIRDaythpqFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCL 476
Cdd:PRK13632 84 KIgiifqNPDNqfIGATveddiafglenKKVPPKKMKD------IIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 477 GKPADVYLIDEPSAYLDSEQRlmaaRVVKRFILH----AKKTAFVVEHDFIMATyLADRVIVFDG 537
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGK----REIKKIMVDlrktRKKTLISITHDMDEAI-LADKVIVFSE 217
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
362-540 |
1.34e-15 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 76.63 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSykPQKISPKS--------------------- 420
Cdd:COG3638 24 LEIERGEFV-----ALIGPSGAGKSTLLRCLNGLVEPTSG-EILVDGQD--VTALRGRAlrrlrrrigmifqqfnlvprl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 421 -------------TGSVRQLLH----EKIRDAYthpqfvtDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVY 483
Cdd:COG3638 96 svltnvlagrlgrTSTWRSLLGlfppEDRERAL-------EALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 484 LIDEPSAYLDSeqrlMAARVVKRFILHA----KKTAFVVEHDFIMATYLADRVI-------VFDGVPS 540
Cdd:COG3638 169 LADEPVASLDP----KTARQVMDLLRRIaredGITVVVNLHQVDLARRYADRIIglrdgrvVFDGPPA 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
350-534 |
1.80e-15 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 79.25 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 350 YPGMKKKMGEFELAIVAGEftdseIMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLN---------VSYKPQK- 415
Cdd:TIGR02857 331 YPGRRPALRPVSFTVPPGE-----RVALVGPSGAGKSTLLNLLLGFVDPTEGsiavNGVPLADadadswrdqIAWVPQHp 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 416 -ISPKST---------GSVRQLLHEKIRDAYTHpQFVTDVmkPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLI 485
Cdd:TIGR02857 406 fLFAGTIaenirlarpDASDAEIREALERAGLD-EFVAAL--PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 108773782 486 DEPSAYLDSEQrlmAARVVKRFILHAK-KTAFVVEHDfIMATYLADRVIV 534
Cdd:TIGR02857 483 DEPTAHLDAET---EAEVLEALRALAQgRTVLLVTHR-LALAALADRIVV 528
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
101-245 |
2.99e-15 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 73.07 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLG--KYDDPPDWQEILTYFRG--------SELQNyfTKILEDDLKAIIKP 170
Cdd:pfam00005 9 NPGEILALVGPNGAGKSTLLKLIAGLLSPTEGtiLLDGQDLTDDERKSLRKeigyvfqdPQLFP--RLTVRENLRLGLLL 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 171 QYVDQIPKAAKgtVGSILDRkdetktqaivcqqLDLTHLKERNVED----LSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:pfam00005 87 KGLSKREKDAR--AEEALEK-------------LGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
373-537 |
5.80e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 72.85 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKStgsvrqllhekIRDAYTHPqfvtdvmkplqIE 452
Cdd:cd03216 27 EVHALLGENGAGKSTLMKILSGLYKPDSG------EILVDGKEVSFAS-----------PRDARRAG-----------IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 453 nIIDQevqtLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRfiLHAKKTAFV-VEHDF--IMAtyLA 529
Cdd:cd03216 79 -MVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR--LRAQGVAVIfISHRLdeVFE--IA 149
|
....*....
gi 108773782 530 DRVIVF-DG 537
Cdd:cd03216 150 DRVTVLrDG 158
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
374-537 |
6.10e-15 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 74.15 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 374 IMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLN--------VSYKPQKISPKSTGSVRQLLH-----EKIRDAY 436
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPSSGtiriDGQDVLKqpqklrrrIGYLPQEFGVYPNFTVREFLDyiawlKGIPSKE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 437 THPQfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCL-GKPaDVYLIDEPSAYLDSEQRLMAARVVKRfiLHAKKTA 515
Cdd:cd03264 107 VKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALvGDP-SILIVDEPTAGLDPEERIRFRNLLSE--LGEDRIV 182
|
170 180
....*....|....*....|..
gi 108773782 516 FVVEHDFIMATYLADRVIVFDG 537
Cdd:cd03264 183 ILSTHIVEDVESLCNQVAVLNK 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
362-537 |
6.78e-15 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 77.95 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVlnvsykpQKISP----KSTGSVRQ---LLHE 430
Cdd:COG2274 496 LTIKPGERV-----AIVGRSGSGKSTLLKLLLGLYEPTSGriliDGIDL-------RQIDPaslrRQIGVVLQdvfLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 431 KIRD--AYTHPQfVTD---------------VMK-PLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYL 492
Cdd:COG2274 564 TIREniTLGDPD-ATDeeiieaarlaglhdfIEAlPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 108773782 493 D--SEQRLMAArvVKRFIlhAKKTAFVVEHDfiMAT-YLADRVIVFDG 537
Cdd:COG2274 643 DaeTEAIILEN--LRRLL--KGRTVIIIAHR--LSTiRLADRIIVLDK 684
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
362-534 |
8.65e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.42 E-value: 8.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLN---VSYKPQKISpKSTGSVRQ--------LLHE 430
Cdd:PRK13548 23 LTLRPGEVV-----AILGPNGAGKSTLLRALSGELSPDSG-EVRLNGrplADWSPAELA-RRRAVLPQhsslsfpfTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 431 KIR-DAYTHPQF-------VTDVMKPLQIENIIDQEVQTLSGGELQRVALA--LC-LGKPAD---VYLIDEPSAYLD--S 494
Cdd:PRK13548 96 VVAmGRAPHGLSraeddalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvLAqLWEPDGpprWLLLDEPTSALDlaH 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 495 EQRLMaaRVVKRFILHAKKTAFVVEHDFIMATYLADRVIV 534
Cdd:PRK13548 176 QHHVL--RLARQLAHERGLAVIVVLHDLNLAARYADRIVL 213
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
100-277 |
1.32e-14 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 74.08 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 100 PRPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDdpPDWQEILTYFRGSELQnyftkileddLKAIIKPQYVDQIPKA 179
Cdd:TIGR03873 24 APPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD--LAGVDLHGLSRRARAR----------RVALVEQDSDTAVPLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 180 AKGTV--GSILDRK----DETKTQAIVCQQL---DLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:TIGR03873 92 VRDVValGRIPHRSlwagDSPHDAAVVDRALartELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVR 171
|
170 180
....*....|....*....|....*..
gi 108773782 251 QRLKAAITIRSLINPDRYIIVVEHDLS 277
Cdd:TIGR03873 172 AQLETLALVRELAATGVTVVAALHDLN 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
102-537 |
1.38e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.51 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGK----------------YDDP------------PDWQEILTYFrgSELQ 153
Cdd:TIGR03719 30 PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgikvgylpqepQLDPtktvrenveegvAEIKDALDRF--NEIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 154 NYFTKIlEDDLKAIIKPQYVDQIPKAAKGtvGSILDRKDETKTQAIVCQQLDLthlkerNVEDLSGGELQRFACAVVCIQ 233
Cdd:TIGR03719 108 AKYAEP-DADFDKLAAEQAELQEIIDAAD--AWDLDSQLEIAMDALRCPPWDA------DVTKLSGGERRRVALCRLLLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 234 KADIFMFDEPSSYLDvkqrlkaAITI----RSLINPDRYIIVVEHDLSVLDYLSDFICCL---YGVP-----SAYgvvtm 301
Cdd:TIGR03719 179 KPDMLLLDEPTNHLD-------AESVawleRHLQEYPGTVVAVTHDRYFLDNVAGWILELdrgRGIPwegnySSW----- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 302 pfsvreginifldgyvptenLRFRDASLvfkvAETANEEEVK----------------------KMCMYKYPGM-----K 354
Cdd:TIGR03719 247 --------------------LEQKQKRL----EQEEKEESARqktlkrelewvrqspkgrqaksKARLARYEELlsqefQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 355 KKMGEFELAIVAGE---------------FTD-------------SEIMVMLGENGTGKTTFIRMLAGRLKPDEG----G 402
Cdd:TIGR03719 303 KRNETAEIYIPPGPrlgdkvieaenltkaFGDklliddlsfklppGGIVGVIGPNGAGKSTLFRMITGQEQPDSGtieiG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 403 EVPVLnvsykpqkispkstGSVRQLlHEKIRDAYTHPQFVTDVMKPLQIENII---------------DQE--VQTLSGG 465
Cdd:TIGR03719 383 ETVKL--------------AYVDQS-RDALDPNKTVWEEISGGLDIIKLGKREipsrayvgrfnfkgsDQQkkVGQLSGG 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 108773782 466 ELQRVALALCLGKPADVYLIDEPSAYLDSEqrlmAARVVKRFILHAKKTAFVVEHDfimaTYLADRV----IVFDG 537
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVE----TLRALEEALLNFAGCAVVISHD----RWFLDRIathiLAFEG 515
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
371-534 |
1.55e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 371 DSEIMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSYK---------PQKISPKSTGSVRQLL------HEK 431
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGTLTPTAGtvlvAGDDVEALSARaasrrvasvPQDTSLSFEFDVRQVVemgrtpHRS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 432 IRDAYTHP--QFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFIl 509
Cdd:PRK09536 108 RFDTWTETdrAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV- 186
|
170 180
....*....|....*....|....*
gi 108773782 510 HAKKTAFVVEHDFIMATYLADRVIV 534
Cdd:PRK09536 187 DDGKTAVAAIHDLDLAARYCDELVL 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
374-575 |
1.62e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.89 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 374 IMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSYK---------PQK-ISPKSTgSVRQLLhEKIRDAYTH- 438
Cdd:PRK11231 30 ITALIGPNGCGKSTLLKCFARLLTPQSGtvflGDKPISMLSSRqlarrlallPQHhLTPEGI-TVRELV-AYGRSPWLSl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 439 --------PQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD-SEQ----RLMaarvvk 505
Cdd:PRK11231 108 wgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDiNHQvelmRLM------ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108773782 506 RFILHAKKTAFVVEHDFIMATYLADRVIVFDGvpsKNTVAN-SPQTLL-AGMNKFLSQLEITFRRDPNNYRP 575
Cdd:PRK11231 182 RELNTQGKTVVTVLHDLNQASRYCDHLVVLAN---GHVMAQgTPEEVMtPGLLRTVFDVEAEIHPEPVSGTP 250
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
352-536 |
1.85e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 72.79 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 352 GMKKKMGEFElAI--VAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDeGGEVPVL-------------NVSYKPQKI 416
Cdd:cd03265 5 NLVKKYGDFE-AVrgVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT-SGRATVAghdvvreprevrrRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 417 S--PKSTGSVRQLLHEKIrdaYTHP-----QFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPS 489
Cdd:cd03265 83 SvdDELTGWENLYIHARL---YGVPgaerrERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 108773782 490 AYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFD 536
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
362-537 |
2.39e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.75 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSykPQKispKSTG------------SVR 425
Cdd:COG3842 26 LSIEPGEF-----VALLGPSGCGKTTLLRMIAGFETPDSGrillDGRDVTGLP--PEK---RNVGmvfqdyalfphlTVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 426 Q-----LLHEKIRDAYTHPQfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCL-GKPaDVYLIDEP-SAyLDSEQRL 498
Cdd:COG3842 96 EnvafgLRMRGVPKAEIRAR-VAELLELVGLEGLADRYPHQLSGGQQQRVALARALaPEP-RVLLLDEPlSA-LDAKLRE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 499 MAARVVKRfILHAKKTAFV-VEHDFIMATYLADRVIVFDG 537
Cdd:COG3842 173 EMREELRR-LQRELGITFIyVTHDQEEALALADRIAVMND 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
352-534 |
3.73e-14 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 72.37 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 352 GMKKKMGEFE-LAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEvpvlNVSYKPqkISPKSTGSVR 425
Cdd:cd03296 7 NVSKRFGDFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGtilfgGE----DATDVP--VQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 426 Q----LLHE----------KIRDAYTHP------QFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLI 485
Cdd:cd03296 81 QhyalFRHMtvfdnvafglRVKPRSERPpeaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 108773782 486 DEPSAYLDSEQRLMAARVVKRfiLHAKK--TAFVVEHDFIMATYLADRVIV 534
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRR--LHDELhvTTVFVTHDQEEALEVADRVVV 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
101-289 |
4.18e-14 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 70.49 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYddppdwqeiltYFRGSELQNYFTKILeddLKAIIkpqYVDQIPKAA 180
Cdd:cd03228 26 KPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-----------LIDGVDLRDLDLESL---RKNIA---YVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTVgsildrkdetktqaivcqqldlthlKErNVedLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK--QRLKAAit 258
Cdd:cd03228 89 SGTI-------------------------RE-NI--LSGGQRQRIAIARALLRDPPILILDEATSALDPEteALILEA-- 138
|
170 180 190
....*....|....*....|....*....|.
gi 108773782 259 IRSLINpDRYIIVVEHDLSVLDyLSDFICCL 289
Cdd:cd03228 139 LRALAK-GKTVIVIAHRLSTIR-DADRIIVL 167
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
354-536 |
5.39e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 73.61 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 354 KKKMGEFELAiVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVpvLNVSYKPQKISP--KSTG---- 422
Cdd:TIGR02142 6 SKRLGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeivlnGRT--LFDSRKGIFLPPekRRIGyvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 423 --------SVRQLL---HEKIRDAYTHPQF--VTDVmkpLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPS 489
Cdd:TIGR02142 83 earlfphlSVRGNLrygMKRARPSERRISFerVIEL---LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 108773782 490 AYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFD 536
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLE 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
362-539 |
5.65e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.04 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVP---------------------VL-NVSYkPQ 414
Cdd:COG1116 32 LTVAAGEFV-----ALVGPSGCGKSTLLRLIAGLEKPTSGevlvdGKPVtgpgpdrgvvfqepallpwltVLdNVAL-GL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 415 KISPKSTGSVRQLLHEKIR--------DAYTHpqfvtdvmkplqieniidqevqTLSGGELQRVALA--LCLgKPaDVYL 484
Cdd:COG1116 106 ELRGVPKAERRERARELLElvglagfeDAYPH----------------------QLSGGMRQRVAIAraLAN-DP-EVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 108773782 485 IDEP-SAyLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVP 539
Cdd:COG1116 162 MDEPfGA-LDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
84-281 |
6.45e-14 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 70.98 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 84 THRYCANAFKLHRLPIP----RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY----DDPPDWQEI-LTYFRGSEL-- 152
Cdd:cd03255 7 SKTYGGGGEKVQALKGVslsiEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgTDISKLSEKeLAAFRRRHIgf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 153 --QNY-----FTkILEDdlkaIIKPQYVDQIPKAakgtvgsildrkdETKTQAI-VCQQLDLTHLKERNVEDLSGGELQR 224
Cdd:cd03255 87 vfQSFnllpdLT-ALEN----VELPLLLAGVPKK-------------ERRERAEeLLERVGLGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 225 FACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRY-IIVVEHDLSVLDY 281
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTtIVVVTHDPELAEY 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
101-290 |
1.36e-13 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 70.54 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELQNyftkileddlkaiIKPQYVD------ 174
Cdd:cd03219 24 RPGEIHGLIGPNGAGKTTLFNLISGFLRPTSG---------SVL--FDGEDITG-------------LPPHEIArlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 --QIPK-------------AA----KGTVGSILDRKDETKTQAIVCQQLD---LTHLKERNVEDLSGGELQRFACAVVCI 232
Cdd:cd03219 80 tfQIPRlfpeltvlenvmvAAqartGSGLLLARARREEREARERAEELLErvgLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 233 QKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLY 290
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLD 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
372-537 |
1.61e-13 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 69.84 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 372 SEIMVMLGENGTGKTTFIRMLAGRLKPDeGGEVPVL-------------NVSYKPQK--ISPKSTgsVRQLL-------- 428
Cdd:cd03263 28 GEIFGLLGHNGAGKTTTLKMLTGELRPT-SGTAYINgysirtdrkaarqSLGYCPQFdaLFDELT--VREHLrfyarlkg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 429 -HEKIRDAYthpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRlmaaRVVKRF 507
Cdd:cd03263 105 lPKSEIKEE-----VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASR----RAIWDL 175
|
170 180 190
....*....|....*....|....*....|...
gi 108773782 508 ILHAKK--TAFVVEHDFIMATYLADRV-IVFDG 537
Cdd:cd03263 176 ILEVRKgrSIILTTHSMDEAEALCDRIaIMSDG 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
102-280 |
1.94e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 67.86 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDwqeiltyfrgselqnyftkileddlkaiIKPQYVDQipkaak 181
Cdd:cd03221 25 PGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------------------------VKIGYFEQ------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 182 gtvgsildrkdetktqaivcqqldlthlkernvedLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRlkAAItIRS 261
Cdd:cd03221 71 -----------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI--EAL-EEA 112
|
170
....*....|....*....
gi 108773782 262 LINPDRYIIVVEHDLSVLD 280
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLD 131
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
362-534 |
2.77e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.14 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVpVLN----VSYKPQKIS------PKSTG-----SVRQ 426
Cdd:COG4559 22 LTLRPGELT-----AIIGPNGAGKSTLLKLLTGELTPSSG-EV-RLNgrplAAWSPWELArrravlPQHSSlafpfTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 L----LHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALA--LC-LGKPADVY----LIDEPSAYLD-- 493
Cdd:COG4559 95 VvalgRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvLAqLWEPVDGGprwlFLDEPTSALDla 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 108773782 494 SEQRLMaaRVVKRFiLHAKKTAFVVEHDFIMATYLADRVIV 534
Cdd:COG4559 175 HQHAVL--RLARQL-ARRGGGVVAVLHDLNLAAQYADRILL 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
362-536 |
3.25e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 72.24 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGrLKPDEG---GEVPV--LNVSYKPQKISPKSTGSVRQ---------- 426
Cdd:COG1123 27 LTIAPGETV-----ALVGESGSGKSTLALALMG-LLPHGGrisGEVLLdgRDLLELSEALRGRRIGMVFQdpmtqlnpvt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 -------------LLHEKIRDAythpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD 493
Cdd:COG1123 101 vgdqiaealenlgLSRAEARAR------VLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 108773782 494 SEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFD 536
Cdd:COG1123 175 VTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMD 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
101-279 |
3.70e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.41 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqeILTYFRGSELQnYFTKILEDDlkaiikpqyvDQIPKAA 180
Cdd:NF040873 16 PAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG----------TVRRAGGARVA-YVPQRSEVP----------DSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTV--------GSI--LDRKDEtktqAIV---CQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYL 247
Cdd:NF040873 75 RDLVamgrwarrGLWrrLTRDDR----AAVddaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 248 DVKQRLKAAITIRSLINPDRYIIVVEHDLSVL 279
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
350-541 |
3.77e-13 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 69.25 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 350 YPGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRQLLH 429
Cdd:TIGR02315 11 YPNGKQALKNINLNINPGEFV-----AIIGPSGAGKSTLLRCINRLVEPSSG------SILLEGTDITKLRGKKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 430 eKIRDAYTHPQFV-----------------------------TDVMKPLQ------IENIIDQEVQTLSGGELQRVALAL 474
Cdd:TIGR02315 80 -RIGMIFQHYNLIerltvlenvlhgrlgykptwrsllgrfseEDKERALSalervgLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 475 CLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRV-------IVFDGVPSK 541
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIvglkageIVFDGAPSE 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
102-287 |
4.31e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 68.48 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGK-------YDD-------PPDWQEILTYFrgselQNY--FTKI-----L 160
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtvLFDsrkkinlPPQQRKIGLVF-----QQYalFPHLnvrenL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 161 EDDLKaiIKPQYVDQIpkaakgTVGSILDRkdetktqaivcqqLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMF 240
Cdd:cd03297 97 AFGLK--RKRNREDRI------SVDELLDL-------------LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 108773782 241 DEPSSYLDVKQRLKAAITIRSLI-NPDRYIIVVEHDLSVLDYLSDFIC 287
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKkNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
101-280 |
4.47e-13 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 72.10 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLG--KYD-------DPPDWQEILTY-------FRGSELQNyftkIL---- 160
Cdd:COG4988 361 PPGERVALVGPSGAGKSTLLNLLLGFLPPYSGsiLINgvdlsdlDPASWRRQIAWvpqnpylFAGTIREN----LRlgrp 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 161 ---EDDLKAIIK----PQYVDQIPkaakgtvgsildrkdetktqaivcQQLDlTHLKERNVEdLSGGELQRFACAVVCIQ 233
Cdd:COG4988 437 dasDEELEAALEaaglDEFVAALP------------------------DGLD-TPLGEGGRG-LSGGQAQRLALARALLR 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 108773782 234 KADIFMFDEPSSYLDVK--QRLKAAitIRSLiNPDRYIIVVEHDLSVLD 280
Cdd:COG4988 491 DAPLLLLDEPTAHLDAEteAEILQA--LRRL-AKGRTVILITHRLALLA 536
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
362-538 |
4.69e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.92 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG-----GE---------------------------VPVL-- 407
Cdd:COG1136 29 LSIEAGEFV-----AIVGPSGSGKSTLLNILGGLDRPTSGevlidGQdisslserelarlrrrhigfvfqffnlLPELta 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 408 --NVSYkPQKISPKSTGSVRQLLHEKIRDaythpqfvtdvmkpLQIENIIDQEVQTLSGGELQRVALALCL-GKPAdvyL 484
Cdd:COG1136 104 leNVAL-PLLLAGVSRKERRERARELLER--------------VGLGDRLDHRPSQLSGGQQQRVAIARALvNRPK---L 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 485 I--DEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYlADRVIVF-DGV 538
Cdd:COG1136 166 IlaDEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLrDGR 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
101-276 |
4.71e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.42 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDDPPdwqeiLTYFRGSELqnyfTKILeddlkAIIkPQY------ 172
Cdd:PRK13548 26 RPGEVVAILGPNGAGKSTLLRALSGELSPDSGEvrLNGRP-----LADWSPAEL----ARRR-----AVL-PQHsslsfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 --VDQIpkAAKG-TVGSILDRKDETKTQAiVCQQLDLTHLKERNVEDLSGGELQR--FACAVVCIQKAD----IFMFDEP 243
Cdd:PRK13548 91 ftVEEV--VAMGrAPHGLSRAEDDALVAA-ALAQVDLAHLAGRDYPQLSGGEQQRvqLARVLAQLWEPDgpprWLLLDEP 167
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 244 SSYLDVKQRLKAAITIRSLINPDRY-IIVVEHDL 276
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERGLaVIVVLHDL 201
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
341-536 |
4.81e-13 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 69.38 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 341 EVKKMCmYKYPGMKKK-MGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSYKpqkiSPK 419
Cdd:TIGR04520 2 EVENVS-FSYPESEKPaLKNVSLSIEKGEFV-----AIIGHNGSGKSTLAKLLNGLLLPTSG-KVTVDGLDTL----DEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 420 STGSVRQLL------------------------------HEKIRdaythpQFVTDVMKPLQIENIIDQEVQTLSGGELQR 469
Cdd:TIGR04520 71 NLWEIRKKVgmvfqnpdnqfvgatveddvafglenlgvpREEMR------KRVDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 470 VALA--LCLgKPaDVYLIDEPSAYLDSEQRLMAARVVKRfiLHAK--KTAFVVEHDFIMATyLADRVIVFD 536
Cdd:TIGR04520 145 VAIAgvLAM-RP-DIIILDEATSMLDPKGRKEVLETIRK--LNKEegITVISITHDMEEAV-LADRVIVMN 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
77-284 |
5.52e-13 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 67.60 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 77 SNLEKETTHRYCANAFKLHrlpIPRpGEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeilTYFRGSELQnyf 156
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLN---IEA-GEIVALLGPSGSGKSTLLRCIAGLEEPDSGS-----------ILIDGEDLT--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 157 tkiledDLKAIIKPQyvdqipkaakgtvgsildrkdETKTqAIVCQQLDL-THLkerNVED-----LSGGELQRFACAVV 230
Cdd:cd03229 66 ------DLEDELPPL---------------------RRRI-GMVFQDFALfPHL---TVLEnialgLSGGQQQRVALARA 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 231 CIQKADIFMFDEPSSYLDVkqrlKAAITIRSLI-----NPDRYIIVVEHDLSVLDYLSD 284
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDP----ITRREVRALLkslqaQLGITVVLVTHDLDEAARLAD 169
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
373-537 |
5.74e-13 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 68.69 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKStGSVRQLLHEKIR----DAYT--HPQF-VTD- 444
Cdd:cd03257 32 ETLGLVGESGSGKSTLARAILGLLKPTSG------SIIFDGKDLLKLS-RRLRKIRRKEIQmvfqDPMSslNPRMtIGEq 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 445 VMKPLQIENIIDQEVQT------------------------LSGGELQRV--ALALCLgKPaDVYLIDEPSAYLDseqrl 498
Cdd:cd03257 105 IAEPLRIHGKLSKKEARkeavllllvgvglpeevlnrypheLSGGQRQRVaiARALAL-NP-KLLIADEPTSALD----- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 108773782 499 maaRVVKRFILH-------AKKTAFV-VEHDFIMATYLADRVIVFDG 537
Cdd:cd03257 178 ---VSVQAQILDllkklqeELGLTLLfITHDLGVVAKIADRVAVMYA 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-537 |
6.67e-13 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 70.13 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 354 KKKMGEFELAiVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVpvLNVSYKPQKISP--KSTG---- 422
Cdd:COG4148 8 RLRRGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGrirlgGEV--LQDSARGIFLPPhrRRIGyvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 423 --------SVRQLL---HEKIRDAYTHPQF--VTDVmkpLQIENIIDQEVQTLSGGELQRVAL--ALcLGKPaDVYLIDE 487
Cdd:COG4148 85 earlfphlSVRGNLlygRKRAPRAERRISFdeVVEL---LGIGHLLDRRPATLSGGERQRVAIgrAL-LSSP-RLLLMDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 488 PSAYLDSE--QRLMA--ARVVKRF---ILHakktafvVEHDFIMATYLADRVIVFDG 537
Cdd:COG4148 160 PLAALDLArkAEILPylERLRDELdipILY-------VSHSLDEVARLADHVVLLEQ 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
369-536 |
7.32e-13 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 67.90 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 369 FTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGeVPVLNVSYKpqkISPKSTGSVRQLLHEKirDAYTHPQFVTDV--- 445
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGR-VLINGVDVT---AAPPADRPVSMLFQEN--NLFAHLTVEQNVglg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 446 ------MKPLQ------------IENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRF 507
Cdd:cd03298 95 lspglkLTAEDrqaievalarvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180
....*....|....*....|....*....
gi 108773782 508 ILHAKKTAFVVEHDFIMATYLADRVIVFD 536
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
374-493 |
8.33e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 8.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 374 IMVMLGENGTGKTTFIRMLAGRLKPDEGG--EVPVLNVSYKPQKISPKSTG--SVRQ--LLHEKIRDAYTHPqfvtdVMK 447
Cdd:PRK09544 32 ILTLLGPNGAGKSTLVRVVLGLVAPDEGVikRNGKLRIGYVPQKLYLDTTLplTVNRflRLRPGTKKEDILP-----ALK 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 108773782 448 PLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD 493
Cdd:PRK09544 107 RVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
360-533 |
8.42e-13 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 67.64 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 360 FELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRQLLHEKI------- 432
Cdd:TIGR03608 17 LNLTIEKGKMY-----AIIGESGSGKSTLLNIIGLLEKFDSG------QVYLNGQETPPLNSKKASKFRREKLgylfqnf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 433 --------------------RDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYL 492
Cdd:TIGR03608 86 alienetveenldlglkykkLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 108773782 493 DSEQRLMAARVVKRfILHAKKTAFVVEHDFIMATyLADRVI 533
Cdd:TIGR03608 166 DPKNRDEVLDLLLE-LNDEGKTIIIVTHDPEVAK-QADRVI 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
373-536 |
8.79e-13 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 68.30 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSYKPQKISPKSTG------------SVRQ---------- 426
Cdd:cd03261 27 EILAIIGPSGSGKSTLLRLIVGLLRPDSGevliDGEDISGLSEAELYRLRRRMGmlfqsgalfdslTVFEnvafplreht 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 -LLHEKIRDaythpqFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSeqrlMAARVVK 505
Cdd:cd03261 107 rLSEEEIRE------IVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP----IASGVID 176
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 506 RFILHAKK----TAFVVEHDFIMATYLADRVIVFD 536
Cdd:cd03261 177 DLIRSLKKelglTSIMVTHDLDTAFAIADRIAVLY 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
102-289 |
9.88e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY---DDPPDW---------QEILTYFRGSELQNYFTKIlEDDLKAIIK 169
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqGKPLDYskrgllalrQQVATVFQDPEQQIFYTDI-DSDIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 170 PQYVDQipkaakgtvGSILDRKDETKTQaivcqqLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:PRK13638 105 NLGVPE---------AEITRRVDEALTL------VDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 250 KQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVL 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
101-287 |
1.02e-12 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 67.53 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeiltyfrgselqnyftkileddlkAIIKPQYVDQIPKAA 180
Cdd:cd03263 26 YKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT--------------------------------AYINGYSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTVGS-----ILD-------------------RKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKAD 236
Cdd:cd03263 74 RQSLGYcpqfdALFdeltvrehlrfyarlkglpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 108773782 237 IFMFDEPSSYLDVkqRLKAAI--TIRSLInPDRYIIVVEHDLSVLDYLSDFIC 287
Cdd:cd03263 154 VLLLDEPTSGLDP--ASRRAIwdLILEVR-KGRSIILTTHSMDEAEALCDRIA 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
349-548 |
1.02e-12 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 68.10 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 349 KYPGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG---------GEVPVL----NVSYKPQK 415
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFL-----VLIGPSGSGKTTTMKMINRLIEPTSGeifidgediREQDPVelrrKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 416 IS--P-----KSTGSVRQLLH---EKIRD-AYTHPQFVTdvmkpLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYL 484
Cdd:cd03295 84 IGlfPhmtveENIALVPKLLKwpkEKIRErADELLALVG-----LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 485 IDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDG-----VPSKNTVANSP 548
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNgeivqVGTPDEILRSP 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
362-536 |
1.34e-12 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 67.65 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSykPQKispKSTGSVRQL---------- 427
Cdd:cd03300 21 LDIKEGEF-----FTLLGPSGCGKTTLLRLIAGFETPTSGeillDGKDITNLP--PHK---RPVNTVFQNyalfphltvf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 428 ------LHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAA 501
Cdd:cd03300 91 eniafgLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQ 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 108773782 502 RVVKRfiLHAK-KTAFV-VEHDFIMATYLADRVIVFD 536
Cdd:cd03300 171 LELKR--LQKElGITFVfVTHDQEEALTMSDRIAVMN 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
101-289 |
2.25e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY---DDPPD-------WQEILTYFRGSELQNYFTkileddlkaiikp 170
Cdd:PRK09536 27 REGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvaGDDVEalsaraaSRRVASVPQDTSLSFEFD------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 171 qyVDQIPKAAKGTVGSILDRKDETKTQAI--VCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:PRK09536 94 --VRQVVEMGRTPHRSRFDTWTETDRAAVerAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 108773782 249 VKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
101-276 |
2.26e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGkQKPNLGK--YDDPPdwqeiLTYFRGSELQNYFTKILEDDLKAIIKP--QYVD-- 174
Cdd:PRK03695 20 RAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSiqFAGQP-----LEAWSAAELARHRAYLSQQQTPPFAMPvfQYLTlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 QIPKAAKGTVGSILDRkdetktqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQ-------KADIFMFDEPSSYL 247
Cdd:PRK03695 94 QPDKTRTEAVASALNE---------VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180 190
....*....|....*....|....*....|.
gi 108773782 248 DVKQrlKAAI--TIRSLINPDRYIIVVEHDL 276
Cdd:PRK03695 165 DVAQ--QAALdrLLSELCQQGIAVVMSSHDL 193
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
105-277 |
2.46e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 66.45 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 105 VLGLVGTNGIGKSTALKILAGKQKPNLGK-----YDDPPDWQEI---LTY----------FRGSELQNYFtkileddlkA 166
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPSSGTiridgQDVLKQPQKLrrrIGYlpqefgvypnFTVREFLDYI---------A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 167 IIKpqyvdQIPKaakgtvgsildrkdeTKTQAIVCQQLDLTHLKERN---VEDLSGGELQRFACAVVCIQKADIFMFDEP 243
Cdd:cd03264 98 WLK-----GIPS---------------KEVKARVDEVLELVNLGDRAkkkIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 108773782 244 SSYLDVKQRlkaaITIRSLI---NPDRYIIVVEHDLS 277
Cdd:cd03264 158 TAGLDPEER----IRFRNLLselGEDRIVILSTHIVE 190
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
371-536 |
2.73e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 66.59 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 371 DSEIMVMLGENGTGKTTFIRMLAGRLKPDEgGEVPVL-NVSYKPQKISPKSTGSV---RQLL---------HEKIRDAYT 437
Cdd:cd03267 46 KGEIVGFIGPNGAGKTTTLKILSGLLQPTS-GEVRVAgLVPWKRRKKFLRRIGVVfgqKTQLwwdlpvidsFYLLAAIYD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 438 HP--QFVTDVMK---PLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDseqrLMAARVVKRFILHAK 512
Cdd:cd03267 125 LPpaRFKKRLDElseLLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD----VVAQENIRNFLKEYN 200
|
170 180
....*....|....*....|....*...
gi 108773782 513 K----TAFVVEHDFIMATYLADRVIVFD 536
Cdd:cd03267 201 RergtTVLLTSHYMKDIEALARRVLVID 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
368-537 |
5.28e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.75 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EFTDSEIMVMLGENGTGKTTFIRMLAGrLKPDEGGEVPVLNVSYKPQKISPKSTGSVRQ-------------------LL 428
Cdd:PRK11000 25 DIHEGEFVVFVGPSGCGKSTLLRMIAG-LEDITSGDLFIGEKRMNDVPPAERGVGMVFQsyalyphlsvaenmsfglkLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 429 HEKIRDAYthpQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRL-MAARVVKrf 507
Cdd:PRK11000 104 GAKKEEIN---QRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVqMRIEISR-- 178
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 508 iLHAK--KTAFVVEHDFIMATYLADRVIVFDG 537
Cdd:PRK11000 179 -LHKRlgRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
349-534 |
5.55e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 349 KYPGMKKKMGEFELAIVAGEftdseIMVMLGENGTGKTTFIRMLAGrLKPDEGGEVpvlnvSYKPQKIS-----PKSTGS 423
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQ-----MVALLGPSGSGKTTLLRIIAG-LEHQTSGHI-----RFHGTDVSrlharDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 424 VRQ-------------------LLHEKIR-DAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVY 483
Cdd:PRK10851 79 VFQhyalfrhmtvfdniafgltVLPRRERpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 108773782 484 LIDEPSAYLDSEQRLMAARVVKRfiLHA--KKTAFVVEHDFIMATYLADRVIV 534
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQ--LHEelKFTSVFVTHDQEEAMEVADRVVV 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
101-286 |
6.39e-12 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 64.34 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEIltyfrgselqnyftKILEDDLKaiikpqyvdQIPKAA 180
Cdd:cd03230 24 EKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG---------EI--------------KVLGKDIK---------KEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTVGSILD--RKDETKTqaiVCQQLdlthlkernveDLSGGELQR--FACAVvcIQKADIFMFDEPSSYLDVKQRLKAA 256
Cdd:cd03230 72 KRRIGYLPEepSLYENLT---VRENL-----------KLSGGMKQRlaLAQAL--LHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|
gi 108773782 257 ITIRSLINPDRYIIVVEHDLSVLDYLSDFI 286
Cdd:cd03230 136 ELLRELKKEGKTILLSSHILEEAERLCDRV 165
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
369-537 |
7.29e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 369 FTDSEIMVMLGENGTGKTTFIRMLaGRLKPDEGGEVpVLN---------------VSYKPQKISPKSTGSVRQLL----- 428
Cdd:PRK10575 34 FPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEI-LLDaqpleswsskafarkVAYLPQQLPAAEGMTVRELVaigry 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 429 -------------HEKIRDAythpqfVTDV-MKPLQieniiDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDS 494
Cdd:PRK10575 112 pwhgalgrfgaadREKVEEA------ISLVgLKPLA-----HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 108773782 495 EQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDG 537
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRG 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
348-553 |
7.50e-12 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 67.87 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKK-MGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVL---------NVSYKP 413
Cdd:COG4987 341 FRYPGAGRPvLDGLSLTLPPGERV-----AIVGPSGSGKSTLLALLLRFLDPQSGsitlGGVDLRdldeddlrrRIAVVP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 414 QKI---SpkstGSVRQ--LLhekIRDAYTHPQfVTDVMKPLQIENIIDQEVQ-----------TLSGGELQRVALALCLG 477
Cdd:COG4987 416 QRPhlfD----TTLREnlRL---ARPDATDEE-LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 478 KPADVYLIDEPSAYLD--SEQRLMAArvvkrfILHA--KKTAFVVEHDFIMATyLADRVIVFDGvpSKNTVANSPQTLLA 553
Cdd:COG4987 488 RDAPILLLDEPTEGLDaaTEQALLAD------LLEAlaGRTVLLITHRLAGLE-RMDRILVLED--GRIVEQGTHEELLA 558
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
373-533 |
8.02e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 64.99 E-value: 8.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpVLNVSYKPQKISPKST-----------------------GSVRQLLH 429
Cdd:cd03269 27 EIFGLLGPNGAGKTTTIRMILGIILPDSG----EVLFDGKPLDIAARNRigylpeerglypkmkvidqlvylAQLKGLKK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 430 EKIRDAythpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSeqrlMAARVVKRFIL 509
Cdd:cd03269 103 EEARRR------IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP----VNVELLKDVIR 172
|
170 180
....*....|....*....|....*..
gi 108773782 510 HAK---KTAFVVEHDFIMATYLADRVI 533
Cdd:cd03269 173 ELAragKTVILSTHQMELVEELCDRVL 199
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
373-502 |
8.55e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 8.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKI-SPKSTGSVRQLLHekiRDAY--------------- 436
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAGLLPPAAG------TIKLDGGDIdDPDVAEACHYLGH---RNAMkpaltvaenlefwaa 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 437 ---THPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSE-----QRLMAAR 502
Cdd:PRK13539 100 flgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAavalfAELIRAH 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
350-534 |
8.80e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 64.74 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 350 YPGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGG-EVPVLNVSYKPQKISPK---STGSVR 425
Cdd:cd03292 10 YPNGTAALDGINISISAGEFV-----FLVGPSGAGKSTLLKLIYKEELPTSGTiRVNGQDVSDLRGRAIPYlrrKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 426 Q----LLHekiRDAYTHPQF---------------VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLID 486
Cdd:cd03292 85 QdfrlLPD---RNVYENVAFalevtgvppreirkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 108773782 487 EPSAYLDSEQRLMAARVVKRFILhAKKTAFVVEHDFIMATYLADRVIV 534
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIA 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
101-535 |
9.54e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 9.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELQnyFTKILeDDLK---AIIkPQYVDQIP 177
Cdd:COG1129 28 RPGEVHALLGENGAGKSTLMKILSGVYQPDSG---------EIL--LDGEPVR--FRSPR-DAQAagiAII-HQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 178 KAakgTV------------GSILDRKDETKTQAIVCQQLDLtHLK-ERNVEDLSGGELQRFACAVVCIQKADIFMFDEPS 244
Cdd:COG1129 93 NL---SVaeniflgreprrGGLIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 245 SYLDVKQ---------RLKAA-ITirslinpdryIIVVEHDLS-VLDyLSDFIcclygvpsaygvvtmpfSVreginifl 313
Cdd:COG1129 169 ASLTEREverlfriirRLKAQgVA----------IIYISHRLDeVFE-IADRV-----------------TV-------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 314 dgyvptenlrFRDASLV--FKVAETaNEEEVKKMcM------YKYPGMKKKMGEFELAI----VAGEFTDSEIMVMLGE- 380
Cdd:COG1129 213 ----------LRDGRLVgtGPVAEL-TEDELVRL-MvgreleDLFPKRAAAPGEVVLEVeglsVGGVVRDVSFSVRAGEi 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 381 ------NGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTG-SVRQ--------------LLHEKIRD----- 434
Cdd:COG1129 281 lgiaglVGAGRTELARALFGADPADSG------EIRLDGKPVRIRSPRdAIRAgiayvpedrkgeglVLDLSIREnitla 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 435 ---AYTHPQFV---------TDVMKPLQIE-NIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD----SE-Q 496
Cdd:COG1129 355 sldRLSRGGLLdrrreralaEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakAEiY 434
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 108773782 497 RLMAArvvkrfiLHAKKTAFVV---EHDFIMAtyLADRVIVF 535
Cdd:COG1129 435 RLIRE-------LAAEGKAVIVissELPELLG--LSDRILVM 467
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
365-494 |
1.01e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 64.98 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 365 VAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDE--GGEVPVLNVSYKPQKiSPKSTGSVRQL--------------- 427
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttSGQILFNGQPRKPDQ-FQKCVAYVRQDdillpgltvretlty 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108773782 428 -----LHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDS 494
Cdd:cd03234 105 tailrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
94-291 |
1.28e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 94 LHRLPIPRP-GEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELQNYFTKILEDDLKAIikPQy 172
Cdd:PRK10575 27 LHPLSLTFPaGKVTGLIGHNGSGKSTLLKMLGRHQPPSEG---------EIL--LDAQPLESWSSKAFARKVAYL--PQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 vdQIPKAAKGTVGSIL-----------------DRKDETKTQAIVcqqlDLTHLKERNVEDLSGGELQRFACAVVCIQKA 235
Cdd:PRK10575 93 --QLPAAEGMTVRELVaigrypwhgalgrfgaaDREKVEEAISLV----GLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 236 DIFMFDEPSSYLDVKQRLKAAITIRSLiNPDR--YIIVVEHDLSVLDYLSDFICCLYG 291
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRL-SQERglTVIAVLHDINMAARYCDYLVALRG 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
368-533 |
1.28e-11 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 63.15 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EFTDSEIMVMLGENGTGKTTFIRMLAgrlkpdeggevpvLNVSYKPQKISPKSTGSVRQLLhekirdAYTHPQFVTdvmk 447
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIG-------------LALGGAQSATRRRSGVKAGCIV------AAVSAELIF---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 448 plqienIIDQevqtLSGGELQRVALALCLG----KPADVYLIDEPSAYLDSEQRLMAARVVKRFILHaKKTAFVVEHDFI 523
Cdd:cd03227 74 ------TRLQ----LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPE 142
|
170
....*....|
gi 108773782 524 MATyLADRVI 533
Cdd:cd03227 143 LAE-LADKLI 151
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
352-537 |
1.30e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 64.09 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 352 GMKKKMGEFE------LAIVAGEftdseIMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSYKPQKISpKST 421
Cdd:cd03262 5 NLHKSFGDFHvlkgidLTVKKGE-----VVVIIGPSGSGKSTLLRCINLLEEPDSGtiiiDGLKLTDDKKNINELR-QKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 422 GSV--------------------RQLLHEKIRDAYTHpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPAD 481
Cdd:cd03262 79 GMVfqqfnlfphltvlenitlapIKVKGMSKAEAEER---ALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 482 VYLIDEPSAYLDSEqrlMAARV--VKRFILHAKKTAFVVEHDFIMATYLADRVIVFDG 537
Cdd:cd03262 156 VMLFDEPTSALDPE---LVGEVldVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
101-277 |
2.19e-11 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 63.69 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDD------PPDWQEILTYFrgselQNYftkILEDDLKAIikpqy 172
Cdd:cd03259 24 EPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilIDGrdvtgvPPERRNIGMVF-----QDY---ALFPHLTVA----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 vDQI---PKAAKGTVGSILDRKDEtktqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:cd03259 91 -ENIafgLKLRGVPKAEIRARVRE------LLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180
....*....|....*....|....*....
gi 108773782 250 KQRLKAAITIRSLI-NPDRYIIVVEHDLS 277
Cdd:cd03259 164 KLREELREELKELQrELGITTIYVTHDQE 192
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
379-537 |
2.51e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 66.34 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 379 GENGTGKTTFIRMLAGRLKPDEG----GEVPVlnvsykpQKISPKS----TGSVRQ---LLHEKIRD--AYTHPQF---- 441
Cdd:COG1132 373 GPSGSGKSTLVNLLLRFYDPTSGriliDGVDI-------RDLTLESlrrqIGVVPQdtfLFSGTIREniRYGRPDAtdee 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 442 VTDVMKPLQIENII-------DQEV----QTLSGGELQRVALA---LclgKPADVYLIDEPSAYLD--SEQRLMAArvVK 505
Cdd:COG1132 446 VEEAAKAAQAHEFIealpdgyDTVVgergVNLSGGQRQRIAIAralL---KDPPILILDEATSALDteTEALIQEA--LE 520
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 506 RfiLHAKKTAFVVEHDF--IMAtylADRVIVFDG 537
Cdd:COG1132 521 R--LMKGRTTIVIAHRLstIRN---ADRILVLDD 549
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
348-536 |
2.59e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.82 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKK-MGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGGEvPVLNVSykPQKISPKSTGSVRq 426
Cdd:PRK13640 13 FTYPDSKKPaLNDISFSIPRGSWT-----ALIGHNGSGKSTISKLINGLLLPDDNPN-SKITVD--GITLTAKTVWDIR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 llhEKIRDAYTHP--QF--------------------------VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGK 478
Cdd:PRK13640 84 ---EKVGIVFQNPdnQFvgatvgddvafglenravprpemikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 479 PADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDfIMATYLADRVIVFD 536
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLD 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
368-537 |
2.62e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.25 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EFTDSEIMVMLGENGTGKTTFIRMLAGrLKPDEGGEV----PVLNvsykpqKISPKSTG--------------SVRQ--- 426
Cdd:PRK11650 26 DVADGEFIVLVGPSGCGKSTLLRMVAG-LERITSGEIwiggRVVN------ELEPADRDiamvfqnyalyphmSVREnma 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 --LlheKIR--DAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVAlalcLG-----KPAdVYLIDEPSAYLDSEQR 497
Cdd:PRK11650 99 ygL---KIRgmPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVA----MGraivrEPA-VFLFDEPLSNLDAKLR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 108773782 498 LmAARV-VKRfiLHA--KKTAFVVEHDFIMATYLADRVIVFDG 537
Cdd:PRK11650 171 V-QMRLeIQR--LHRrlKTTSLYVTHDQVEAMTLADRVVVMNG 210
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
102-495 |
3.18e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY------------DDPPDWQEILTYFRGSELQNYFTKILED--DLKAI 167
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarlqQDPPRNVEGTVYDFVAEGIEEQAEYLKRyhDISHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 168 IKPQYVDQ-IPKAAKgtVGSILDRKD----ETKTQAiVCQQLDLThlKERNVEDLSGGELQRFACAVVCIQKADIFMFDE 242
Cdd:PRK11147 108 VETDPSEKnLNELAK--LQEQLDHHNlwqlENRINE-VLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 243 PSSYLDVKqrlkaaiTI----RSLINPDRYIIVVEHDLSVLDYLSDFICCL-YGVpsaygVVTMPFSVregiNIFLDGyv 317
Cdd:PRK11147 183 PTNHLDIE-------TIewleGFLKTFQGSIIFISHDRSFIRNMATRIVDLdRGK-----LVSYPGNY----DQYLLE-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 318 PTENLR---FRDASLVFKVAE-------------TANEEEV---KKMCMYKYP------GMKKKMGE--------FELAI 364
Cdd:PRK11147 245 KEEALRveeLQNAEFDRKLAQeevwirqgikarrTRNEGRVralKALRRERSErrevmgTAKMQVEEasrsgkivFEMEN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 365 VAGEFTDSEIM------VM-------LGENGTGKTTFIRMLAGRLKPDEgGEVPV---LNVSYKPQ---KISPKST---- 421
Cdd:PRK11147 325 VNYQIDGKQLVkdfsaqVQrgdkialIGPNGCGKTTLLKLMLGQLQADS-GRIHCgtkLEVAYFDQhraELDPEKTvmdn 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 422 -----------GSVRQLLhEKIRDAYTHPQfvtDVMKPlqieniidqeVQTLSGGELQRVALALCLGKPADVYLIDEPSA 490
Cdd:PRK11147 404 laegkqevmvnGRPRHVL-GYLQDFLFHPK---RAMTP----------VKALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
....*
gi 108773782 491 YLDSE 495
Cdd:PRK11147 470 DLDVE 474
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
368-561 |
3.38e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EFTDSEIMVMLGENGTGKTTFIRMLaGRLKPDEGGEVPVLNVSYKPQKISPKSTGSVRQLLHE-----KIRDAYTHPQFV 442
Cdd:PRK11264 25 EVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQLRQHvgfvfQNFNLFPHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 443 TDVMK-PLQIENIIDQEV---------------------QTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEqrlMA 500
Cdd:PRK11264 104 ENIIEgPVIVKGEPKEEAtararellakvglagketsypRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE---LV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 501 ARVVK--RFILHAKKTAFVVEHDFIMATYLADRVIVFD-GV-----PSKNTVAN--SPQTLLAgMNKFLSQ 561
Cdd:PRK11264 181 GEVLNtiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDqGRiveqgPAKALFADpqQPRTRQF-LEKFLLQ 250
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
348-536 |
3.40e-11 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 62.33 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKK-MGEFELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVsykpQKISPKSTG 422
Cdd:cd03247 8 FSYPEQEQQvLKNLSLELKQGEK-----IALLGRSGSGKSTLLQLLTGDLKPQQGeitlDGVPVSDL----EKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 423 SVRQLLHekirdaythpQFVTDVMkplqiENIIDQevqtLSGGELQRVALALCLGKPADVYLIDEPSAYLD--SEQRLMa 500
Cdd:cd03247 79 VLNQRPY----------LFDTTLR-----NNLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDpiTERQLL- 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 108773782 501 arvvKRFILHAK-KTAFVVEHDFIMATYlADRVIVFD 536
Cdd:cd03247 139 ----SLIFEVLKdKTLIWITHHLTGIEH-MDKILFLE 170
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
101-275 |
5.06e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDdppdwqeiltyfRGSELQ-NYFTK---ILEDDLKAI--IKPQYVD 174
Cdd:COG0488 339 DRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK------------LGETVKiGYFDQhqeELDPDKTVLdeLRDGAPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 QIPKAAKGTVGSILDRKDETKTQaivcqqldlthlkernVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKqrlk 254
Cdd:COG0488 407 GTEQEVRGYLGRFLFSGDDAFKP----------------VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE---- 466
|
170 180
....*....|....*....|....*
gi 108773782 255 aaiTIRSLINP-DRY---IIVVEHD 275
Cdd:COG0488 467 ---TLEALEEAlDDFpgtVLLVSHD 488
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
101-279 |
5.29e-11 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 65.63 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YD-------DPPDWQEILTY-------FRGSELQNyftkIleddl 164
Cdd:COG2274 499 KPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilIDgidlrqiDPASLRRQIGVvlqdvflFSGTIREN----I----- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 165 kAIIKPQY-VDQIPKAAKgTVGsiLDrkDETKTQAivcQQLDlTHLKERNvEDLSGGELQRFACAVVCIQKADIFMFDEP 243
Cdd:COG2274 570 -TLGDPDAtDEEIIEAAR-LAG--LH--DFIEALP---MGYD-TVVGEGG-SNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 108773782 244 SSYLD------VKQRLKAaitirslINPDRYIIVVEHDLSVL 279
Cdd:COG2274 639 TSALDaeteaiILENLRR-------LLKGRTVIIIAHRLSTI 673
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
101-289 |
5.64e-11 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 61.56 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeilTYFRGSELQNYftkilEDDLKAIIKpqYVDQIPKAA 180
Cdd:cd03247 26 KQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE-----------ITLDGVPVSDL-----EKALSSLIS--VLNQRPYLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTVGSILDRKdetktqaivcqqldlthlkernvedLSGGELQRFACAVVCIQKADIFMFDEPSSYLDvkqrlkaAITIR 260
Cdd:cd03247 88 DTTLRNNLGRR-------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLD-------PITER 135
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 261 SLIN------PDRYIIVVEHDLSVLDYLsDFICCL 289
Cdd:cd03247 136 QLLSlifevlKDKTLIWITHHLTGIEHM-DKILFL 169
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
102-257 |
5.88e-11 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 62.11 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--------YDDPPDWQEILTYFrGSELQnyftkiLEDDLKAIikpQYV 173
Cdd:COG4133 27 AGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepiRDAREDYRRRLAYL-GHADG------LKPELTVR---ENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 174 DQIpKAAKGTVGSildrkDETKTQAIvcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK--Q 251
Cdd:COG4133 97 RFW-AALYGLRAD-----REAIDEAL--EAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAgvA 168
|
....*.
gi 108773782 252 RLKAAI 257
Cdd:COG4133 169 LLAELI 174
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
377-537 |
6.59e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.67 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 377 MLGENGTGKTTFIRMLAGRLKPDEG-----GEvPV--------LNVSYKPQKISPKSTGSVRQLLHEKIR----DAYTHP 439
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGsislcGE-PVpsrarharQRVGVVPQFDNLDPDFTVRENLLVFGRyfglSAAAAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 440 QFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQR-LMAARVvkRFILHAKKTAFVV 518
Cdd:PRK13537 117 ALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARhLMWERL--RSLLARGKTILLT 194
|
170
....*....|....*....
gi 108773782 519 EHDFIMATYLADRVIVFDG 537
Cdd:PRK13537 195 THFMEEAERLCDRLCVIEE 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
362-534 |
7.70e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 62.38 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFtdseimVML-GENGTGKTTFIRMLAGRLKPDEG--------------GEVPVL------------------- 407
Cdd:COG2884 23 LEIEKGEF------VFLtGPSGAGKSTLLKLLYGEERPTSGqvlvngqdlsrlkrREIPYLrrrigvvfqdfrllpdrtv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 408 --NVSYkPQKISPKStgsvrqllHEKIRDAythpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVAL--ALcLGKPaDVY 483
Cdd:COG2884 97 yeNVAL-PLRVTGKS--------RKEIRRR------VREVLDLVGLSDKAKALPHELSGGEQQRVAIarAL-VNRP-ELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 484 LIDEPSAYLDSEqrlMAARVVKRFI-LHAKKTAfvvehdFIMATYlaDRVIV 534
Cdd:COG2884 160 LADEPTGNLDPE---TSWEIMELLEeINRRGTT------VLIATH--DLELV 200
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
353-560 |
7.75e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.68 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 353 MKKKMGEFE-LAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGevpvLNVSYKPQKISPKSTGSVR------ 425
Cdd:PRK10619 11 LHKRYGEHEvLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGS----IVVNGQTINLVRDKDGQLKvadknq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 426 -QLLHEKIR------DAYTHPQFVTDVMK-PLQIENIIDQEVQT----------------------LSGGELQRVALALC 475
Cdd:PRK10619 87 lRLLRTRLTmvfqhfNLWSHMTVLENVMEaPIQVLGLSKQEAREravkylakvgideraqgkypvhLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 476 LGKPADVYLIDEPSAYLDSEQRLMAARVVKRfILHAKKTAFVVEHDFIMATYLADRVIVF-------DGVPSKntVANSP 548
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVIFLhqgkieeEGAPEQ--LFGNP 243
|
250
....*....|..
gi 108773782 549 QTllAGMNKFLS 560
Cdd:PRK10619 244 QS--PRLQQFLK 253
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
102-249 |
7.98e-11 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 62.00 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGK-----YD---DPPDWQEILTYFRGSELqnyftkiLEDDLKAIIKPQYV 173
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgFDvvkEPAEARRRLGFVSDSTG-------LYDRLTARENLEYF 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 108773782 174 DQIpKAAKGTvgSILDRKDEtktqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:cd03266 103 AGL-YGLKGD--ELTARLEE------LADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
97-275 |
1.08e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 61.50 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 97 LPIPRpGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY--------DDPPDWQEILTYFrgselQNYftkileddlkaII 168
Cdd:cd03301 21 LDIAD-GEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtDLPPKDRDIAMVF-----QNY-----------AL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 169 KPQYV--DQI--PKAAKGTVGSILDRKDETktqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPS 244
Cdd:cd03301 84 YPHMTvyDNIafGLKLRKVPKDEIDERVRE-----VAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 245 SYLDVKQRLKAAITIRSL-INPDRYIIVVEHD 275
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLqQRLGTTTIYVTHD 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
373-520 |
1.11e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.93 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQK--ISPkstGSVRqllhEKIRDAYTHPQF-VTDVMKPL 449
Cdd:TIGR01271 453 QLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTswIMP---GTIK----DNIIFGLSYDEYrYTSVIKAC 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 450 QIENII------DQEVQ-----TLSGGELQRVALALCLGKPADVYLIDEPSAYLD--SEQRLMAARVVKrfiLHAKKTAF 516
Cdd:TIGR01271 526 QLEEDIalfpekDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEKEIFESCLCK---LMSNKTRI 602
|
....*...
gi 108773782 517 VV----EH 520
Cdd:TIGR01271 603 LVtsklEH 610
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
371-538 |
1.24e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 62.28 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 371 DSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEvPVLNVSYKP-QKISPKSTGSVRQ----LLHEKIRDAYTHP- 439
Cdd:cd03294 49 EGEIFVIMGLSGSGKSTLLRCINRLIEPTSGkvlidGQ-DIAAMSRKElRELRRKKISMVFQsfalLPHRTVLENVAFGl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 440 -----------QFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRL-MAARVVKrf 507
Cdd:cd03294 128 evqgvpraereERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRReMQDELLR-- 205
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 508 iLHAK--KTAFVVEHDFIMATYLADRV-IVFDGV 538
Cdd:cd03294 206 -LQAElqKTIVFITHDLDEALRLGDRIaIMKDGR 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
101-297 |
1.25e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 61.53 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDDPPDWQEILTYF------RGselqnyftkiLEDDLKAIIKPQY 172
Cdd:cd03269 24 EKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEvlFDGKPLDIAARNRIgylpeeRG----------LYPKMKVIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VDQI----PKAAKGTVGSILDRkdetktqaivcqqLDLTHLKERNVEDLSGGELQR--FACAVvcIQKADIFMFDEPSSY 246
Cdd:cd03269 94 LAQLkglkKEEARRRIDEWLER-------------LELSEYANKRVEELSKGNQQKvqFIAAV--IHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 108773782 247 LD-VKQRLKAAItIRSLINPDRYIIVVEHDLSVLDYLSDFICCLY-GVPSAYG 297
Cdd:cd03269 159 LDpVNVELLKDV-IRELARAGKTVILSTHQMELVEELCDRVLLLNkGRAVLYG 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
360-503 |
1.38e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.84 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 360 FELAivAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEG------------GEVPVLNVSYKPQKISPKSTGSVRQL 427
Cdd:TIGR01189 21 FTLN--AGEA-----LQVTGPNGIGKTTLLRILAGLLRPDSGevrwngtplaeqRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 428 LHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSE-QRLMAARV 503
Cdd:TIGR01189 94 LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAgVALLAGLL 170
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
335-538 |
1.57e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 335 ETANEEEVKKMCM------YKYPGMKKKMGEFELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEG-----GE 403
Cdd:PRK09452 2 KKLNKQPSSLSPLvelrgiSKSFDGKEVISNLDLTINNGEF-----LTLLGPSGCGKTTVLRLIAGFETPDSGrimldGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 404 vpvlNVSYKPQKISPKST----------GSVRQ-----LLHEKIRDAYTHPQfVTDVMKPLQIENIIDQEVQTLSGGELQ 468
Cdd:PRK09452 77 ----DITHVPAENRHVNTvfqsyalfphMTVFEnvafgLRMQKTPAAEITPR-VMEALRMVQLEEFAQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108773782 469 RVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRfiLHAK-KTAFV-VEHDFIMATYLADRVIVF-DGV 538
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKA--LQRKlGITFVfVTHDQEEALTMSDRIVVMrDGR 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
348-553 |
1.74e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.93 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKKMGEFELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPdEGGEVPVLNVSykpqKISPKSTGSVRQL 427
Cdd:PRK13644 9 YSYPDGTPALENINLVIKKGEY-----IGIIGKNGSGKSTLALHLNGLLRP-QKGKVLVSGID----TGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 428 LHEKIRDAYThpQFVTDVMK-------------PLQIENIIDQEV-------------QTLSGGELQRVALALCLGKPAD 481
Cdd:PRK13644 79 VGIVFQNPET--QFVGRTVEedlafgpenlclpPIEIRKRVDRALaeiglekyrhrspKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108773782 482 VYLIDEPSAYLDSEQRLMAARVVKRfiLHAK-KTAFVVEHDfIMATYLADRVIVFDgvPSKNTVANSPQTLLA 553
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKK--LHEKgKTIVYITHN-LEELHDADRIIVMD--RGKIVLEGEPENVLS 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
334-501 |
1.74e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 63.71 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 334 AETANEEEVKKMCMYKYPGmKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLkPDEGG------EVPVL 407
Cdd:PRK11174 344 SNDPVTIEAEDLEILSPDG-KTLAGPLNFTLPAGQRI-----ALVGPSGAGKTSLLNALLGFL-PYQGSlkingiELREL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 408 NVSYKPQKIS-----PkstgsvrQLLHEKIRDAYT------HPQFVTDVMKPLQIENIIDQEVQ-----------TLSGG 465
Cdd:PRK11174 417 DPESWRKHLSwvgqnP-------QLPHGTLRDNVLlgnpdaSDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVG 489
|
170 180 190
....*....|....*....|....*....|....*...
gi 108773782 466 ELQRVALALCLGKPADVYLIDEPSAYLD--SEQRLMAA 501
Cdd:PRK11174 490 QAQRLALARALLQPCQLLLLDEPTASLDahSEQLVMQA 527
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
373-536 |
2.67e-10 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 60.76 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEgGEVPVLNVSYkpqkispkSTGSVRQLlhEKIR-------------DAYThp 439
Cdd:COG1127 32 EILAIIGGSGSGKSVLLKLIIGLLRPDS-GEILVDGQDI--------TGLSEKEL--YELRrrigmlfqggalfDSLT-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 440 qfVTD-VMKPLQI-----ENIIDQEVQT-----------------LSGGELQRVALA--LCLgKPaDVYLIDEPSAYLDS 494
Cdd:COG1127 99 --VFEnVAFPLREhtdlsEAEIRELVLEklelvglpgaadkmpseLSGGMRKRVALAraLAL-DP-EILLYDEPTAGLDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 108773782 495 EqrlmAARVVKRFILHAKK----TAFVVEHDFIMATYLADRVIVFD 536
Cdd:COG1127 175 I----TSAVIDELIRELRDelglTSVVVTHDLDSAFAIADRVAVLA 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
373-550 |
2.86e-10 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 60.75 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG---------GEVPV-----LNVSYKPQKISPKSTGSVRQ-----LLHEKIR 433
Cdd:TIGR04406 28 EIVGLLGPNGAGKTTSFYMIVGLVRPDAGkilidgqdiTHLPMherarLGIGYLPQEASIFRKLTVEEnimavLEIRKDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 434 DAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSeqrlMAARVVKRFILH--- 510
Cdd:TIGR04406 108 DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDP----IAVGDIKKIIKHlke 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 108773782 511 -----------AKKTAFVVEHDFIMatylADRVIVFDGVPSknTVANSPQT 550
Cdd:TIGR04406 184 rgigvlitdhnVRETLDICDRAYII----SDGKVLAEGTPA--EIVANEKV 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
362-534 |
3.02e-10 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 59.54 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPdeggevpvlnvsykpqkispkSTGSVRqLLHEKIRDAY--THP 439
Cdd:cd03246 23 FSIEPGESL-----AIIGPSGSGKSTLARLILGLLRP---------------------TSGRVR-LDGADISQWDpnELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 440 QFVTDVMKPLQ------IENIidqevqtLSGGELQRVALALCL-GKPADVYLiDEPSAYLDS--EQRLMAArvvkrfILH 510
Cdd:cd03246 76 DHVGYLPQDDElfsgsiAENI-------LSGGQRQRLGLARALyGNPRILVL-DEPNSHLDVegERALNQA------IAA 141
|
170 180
....*....|....*....|....*...
gi 108773782 511 AKK---TAFVVEHDfiMATY-LADRVIV 534
Cdd:cd03246 142 LKAagaTRIVIAHR--PETLaSADRILV 167
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
9-72 |
3.11e-10 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 56.66 E-value: 3.11e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 9 AIVNHDKCKpkKCRQeCKKSCPVvrmgkLCIEVTpqSKIAWISETLCIGCGICIKKCPFGALSI 72
Cdd:COG2768 6 PYVDEEKCI--GCGA-CVKVCPV-----GAISIE--DGKAVIDPEKCIGCGACIEVCPVGAIKI 59
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
373-535 |
3.49e-10 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 60.27 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAG-----RLKPDEG----GEVPVLNVSYKPQKIsPKSTGSVRQ---LLHEKIRD--AYth 438
Cdd:cd03260 27 EITALIGPSGCGKSTLLRLLNRlndliPGAPDEGevllDGKDIYDLDVDVLEL-RRRVGMVFQkpnPFPGSIYDnvAY-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 439 pqfvtdvmkPLQI-----ENIIDQEVQT-------------------LSGGELQRVALALCLGKPADVYLIDEPSAYLDS 494
Cdd:cd03260 104 ---------GLRLhgiklKEELDERVEEalrkaalwdevkdrlhalgLSGGQQQRLCLARALANEPEVLLLDEPTSALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 108773782 495 EqrlmAARVVKRFILHAKK--TAFVVEHDFIMATYLADRVIVF 535
Cdd:cd03260 175 I----STAKIEELIAELKKeyTIVIVTHNMQQAARVADRTAFL 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
373-518 |
3.61e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.03 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQK--ISPkstGSVRqllhEKIRDAYTHPQF-VTDVMKPL 449
Cdd:cd03291 64 EMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFswIMP---GTIK----ENIIFGVSYDEYrYKSVVKAC 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 450 QIENII------DQEVQ-----TLSGGELQRVALALCLGKPADVYLIDEPSAYLD--SEQRLMAARVVKrfiLHAKKTAF 516
Cdd:cd03291 137 QLEEDItkfpekDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfTEKEIFESCVCK---LMANKTRI 213
|
..
gi 108773782 517 VV 518
Cdd:cd03291 214 LV 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
102-284 |
3.72e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.88 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEI-------LTYFRGSELQnyFTKILEDDLK--AIIKPQY 172
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSG---------EIglakgikLGYFAQHQLE--FLRADESPLQhlARLAPQE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VDQIPKAAKGTVGSILDRKDEtktqaivcqqldlthlkerNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQR 252
Cdd:PRK10636 406 LEQKLRDYLGGFGFQGDKVTE-------------------ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 253 lkAAITiRSLINPDRYIIVVEHDLSVLDYLSD 284
Cdd:PRK10636 467 --QALT-EALIDFEGALVVVSHDRHLLRSTTD 495
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-541 |
3.77e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.18 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKK-KMGEFELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRq 426
Cdd:PRK13635 13 FRYPDAATyALKDVSFSVYEGEW-----VAIVGHNGSGKSTLAKLLNGLLLPEAG------TITVGGMVLSEETVWDVR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 llhEKIRDAYTHP--QFV-----TDV---------------------MKPLQIENIIDQEVQTLSGGELQRVALALCLGK 478
Cdd:PRK13635 81 ---RQVGMVFQNPdnQFVgatvqDDVafglenigvpreemvervdqaLRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 479 PADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYlADRVIVFD-------GVPSK 541
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNkgeileeGTPEE 226
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
373-535 |
4.44e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.87 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRmlagrlkpdEGGEVPVLNVSYK-PQKISPKSTGSVRQLlhekirdaythpQFVTDVmkplqi 451
Cdd:cd03238 22 VLVVVTGVSGSGKSTLVN---------EGLYASGKARLISfLPKFSRNKLIFIDQL------------QFLIDV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 452 eNI----IDQEVQTLSGGELQRVALALCLGKPAD--VYLIDEPSAYLDSEQRLMAARVVKRfILHAKKTAFVVEHDFIMA 525
Cdd:cd03238 75 -GLgyltLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG-LIDLGNTVILIEHNLDVL 152
|
170
....*....|
gi 108773782 526 TYlADRVIVF 535
Cdd:cd03238 153 SS-ADWIIDF 161
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
336-566 |
5.27e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.52 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 336 TANEEEVKKMcMYKYpgmKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPD------EGGEVPVLNV 409
Cdd:PRK13650 1 MSNIIEVKNL-TFKY---KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsgqiiiDGDLLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 410 SYKPQKISPKSTGSVRQLLHEKIRD---------AYTHPQFVTDVMKPLQI---ENIIDQEVQTLSGGELQRVALALCLG 477
Cdd:PRK13650 77 WDIRHKIGMVFQNPDNQFVGATVEDdvafglenkGIPHEEMKERVNEALELvgmQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 478 KPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATyLADRVIVF-DG-VPSKNTvansPQTLLAGM 555
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMkNGqVESTST----PRELFSRG 231
|
250
....*....|..
gi 108773782 556 NKFLS-QLEITF 566
Cdd:PRK13650 232 NDLLQlGLDIPF 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
373-536 |
5.73e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.39 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG---------GEVPV----LNVSYKPQKISPKSTgsVRQ-----LLHEKIRD 434
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQPTAGqimldgvdlSHVPPyqrpINMMFQSYALFPHMT--VEQniafgLKQDKLPK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 435 AYTHPQfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQR-LMAARVVKrfILH-AK 512
Cdd:PRK11607 124 AEIASR-VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdRMQLEVVD--ILErVG 200
|
170 180
....*....|....*....|....
gi 108773782 513 KTAFVVEHDFIMATYLADRVIVFD 536
Cdd:PRK11607 201 VTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
351-540 |
6.73e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 351 PGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSyKPQKISP--KSTGSV 424
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYT-----ALIGHTGSGKSTLLQHLNGLLQPTEGkvtvGDIVVSSTS-KQKEIKPvrKKVGVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 425 -----RQLLHEKI-RDAYTHPQFVTdvMKPLQIENIIDQEVQT--------------LSGGELQRVALALCLGKPADVYL 484
Cdd:PRK13643 90 fqfpeSQLFEETVlKDVAFGPQNFG--IPKEKAEKIAAEKLEMvgladefwekspfeLSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108773782 485 IDEPSAYLDSEQRLMAARVVKRfILHAKKTAFVVEH------DFIMATYLADR-VIVFDGVPS 540
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHlmddvaDYADYVYLLEKgHIISCGTPS 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
101-286 |
6.92e-10 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 59.56 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDD------PPDWQEILTYFrgselQNYftkileddlkAIIKPQY 172
Cdd:cd03300 24 KEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEilLDGkditnlPPHKRPVNTVF-----QNY----------ALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 V-DQIPKAAKgtvgsiLDRKDETKTQAIVCQQLDLTHLKE---RNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:cd03300 89 VfENIAFGLR------LKKLPKAEIKERVAEALDLVQLEGyanRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 108773782 249 VKQRLKAAITIRSL-----INpdryIIVVEHDLSVLDYLSDFI 286
Cdd:cd03300 163 LKLRKDMQLELKRLqkelgIT----FVFVTHDQEEALTMSDRI 201
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
373-537 |
7.26e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 60.20 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQ---KISPKSTGSVRQLLHEKIRDAYT--HPQ------- 440
Cdd:TIGR02769 38 ETVGLLGRSGCGKSTLARLLLGLEKPAQG------TVSFRGQdlyQLDRKQRRAFRRDVQLVFQDSPSavNPRmtvrqii 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 441 -----FVTDVMKPLQIENI-------------IDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAAR 502
Cdd:TIGR02769 112 geplrHLTSLDESEQKARIaelldmvglrsedADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILE 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 108773782 503 VVKRfILHAKKTAFV-VEHDFIMATYLADRVIVFDG 537
Cdd:TIGR02769 192 LLRK-LQQAFGTAYLfITHDLRLVQSFCQRVAVMDK 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
373-493 |
7.38e-10 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 59.48 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GE----VPV-----LNVSYKPQKISPKSTGSVRQ---LLHEKIRDA 435
Cdd:cd03218 27 EIVGLLGPNGAGKTTTFYMIVGLVKPDSGkilldGQditkLPMhkrarLGIGYLPQEASIFRKLTVEEnilAVLEIRGLS 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 436 YTHPQFVTD-VMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD 493
Cdd:cd03218 107 KKEREEKLEeLLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
9-73 |
8.91e-10 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 55.05 E-value: 8.91e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 9 AIVNHDKCKpkKCRqECKKSCPVvrmgklcIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIV 73
Cdd:COG4231 17 YVIDEDKCT--GCG-ACVKVCPA-------DAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKLE 71
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
373-533 |
9.30e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSYK-PQKISPKSTGSVRQLL-----------HEKIRDAYTH-P 439
Cdd:COG4161 29 ETLVLLGPSGAGKSSLLRVLNLLETPDSG-QLNIAGHQFDfSQKPSEKAIRLLRQKVgmvfqqynlwpHLTVMENLIEaP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 440 QFVTDVMKP------------LQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEqrlMAARVVKrF 507
Cdd:COG4161 108 CKVLGLSKEqarekamkllarLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE---ITAQVVE-I 183
|
170 180
....*....|....*....|....*....
gi 108773782 508 ILHAKKTAF---VVEHDFIMATYLADRVI 533
Cdd:COG4161 184 IRELSQTGItqvIVTHEVEFARKVASQVV 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
359-517 |
9.83e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 57.55 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 359 EFELAIVAGEftdsEIMVMlGENGTGKTTFIRMLAGrLKPDEGGEV---PVLNVSYKPQKisPK-STGSVRQLLhekird 434
Cdd:cd03223 19 DLSFEIKPGD----RLLIT-GPSGTGKSSLFRALAG-LWPWGSGRIgmpEGEDLLFLPQR--PYlPLGTLREQL------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 435 AYthpqfvtdvmkPLQieniidqevQTLSGGELQRVALA-LCLGKPaDVYLIDEPSAYLD--SEQRLMAarvvkrfILHA 511
Cdd:cd03223 85 IY-----------PWD---------DVLSGGEQQRLAFArLLLHKP-KFVFLDEATSALDeeSEDRLYQ-------LLKE 136
|
....*.
gi 108773782 512 KKTAFV 517
Cdd:cd03223 137 LGITVI 142
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
103-284 |
1.13e-09 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 58.89 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKY--------DDPPDWQEIltyfrGSELQNY--FTKI-LEDDLKAIIKPQ 171
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkditNLPPEKRDI-----SYVPQNYalFPHMtVYKNIAYGLKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 172 YVDQIPKAAKgtvgsILDrkdetktqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQ 251
Cdd:cd03299 100 KVDKKEIERK-----VLE----------IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 252 RLKAAITIRSLI-NPDRYIIVVEHDLSVLDYLSD 284
Cdd:cd03299 165 KEKLREELKKIRkEFGVTVLHVTHDFEEAWALAD 198
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
3-74 |
1.24e-09 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 60.81 E-value: 1.24e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108773782 3 DKLTRIAIVNHDKCKpkKCRQeCKKSCPVVRMGKlcievtpQSKIAWISETLCIGCGICIKKCPFGALSIVN 74
Cdd:COG4624 80 DKRGPSIIRDKEKCK--NCYP-CVRACPVKAIKV-------DDGKAEIDEEKCISCGQCVAVCPFGAITEKS 141
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
359-501 |
1.37e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.98 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 359 EFELAIVAGEFtdseIMVMlGENGTGKTTFIRMLAGrLKPDEGGEV---PVLNVSYKPQKisPK-STGSVR-QLLHEKIR 433
Cdd:COG4178 381 DLSLSLKPGER----LLIT-GPSGSGKSTLLRAIAG-LWPYGSGRIarpAGARVLFLPQR--PYlPLGTLReALLYPATA 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 434 DAYTHPQfVTDVMKPLQIENII---DQEV---QTLSGGELQRVALA-LCLGKPADVYLiDEPSAYLD--SEQRLMAA 501
Cdd:COG4178 453 EAFSDAE-LREALEAVGLGHLAerlDEEAdwdQVLSLGEQQRLAFArLLLHKPDWLFL-DEATSALDeeNEAALYQL 527
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
101-303 |
1.49e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 58.63 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLG-------KYDDP-PDwqeiltyfRGSELQNYftkileddlkAIIKPQY 172
Cdd:TIGR01184 9 QQGEFISLIGHSGCGKSTLLNLISGLAQPTSGgvilegkQITEPgPD--------RMVVFQNY----------SLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VDQIPKAAkgtVGSILDRKDETKTQAIVCQQLD---LTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:TIGR01184 71 VRENIALA---VDRVLPDLSKSERRAIVEEHIAlvgLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 250 KQRLKAAITIRSLINPDR-YIIVVEHDLSVLDYLSDFICCLYGVPSAY--GVVTMPF 303
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANigQILEVPF 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
378-536 |
1.57e-09 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 58.31 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 378 LGENGTGKTTFIRMLAGRLKPDEG-----GEV-PVLNVSYKpqkISPKSTG--------SV----RQLLHEKIRDAYthp 439
Cdd:cd03220 54 IGRNGAGKSTLLRLLAGIYPPDSGtvtvrGRVsSLLGLGGG---FNPELTGreniylngRLlglsRKEIDEKIDEII--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 440 QFVtdvmkplQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAkKTAFVVE 519
Cdd:cd03220 128 EFS-------ELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQG-KTVILVS 199
|
170
....*....|....*..
gi 108773782 520 HDFIMATYLADRVIVFD 536
Cdd:cd03220 200 HDPSSIKRLCDRALVLE 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
373-536 |
1.62e-09 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 58.21 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTgsvrqllHEKIRD--AYThPQ---------- 440
Cdd:cd03224 27 EIVALLGRNGAGKTTLLKTIMGLLPPRSG------SIRFDGRDITGLPP-------HERARAgiGYV-PEgrrifpeltv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 441 ---------FVTDVMKPLQIENIID----------QEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLdseQRLMAA 501
Cdd:cd03224 93 eenlllgayARRRAKRKARLERVYElfprlkerrkQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL---APKIVE 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 108773782 502 RVVKRFI-LHAKKTA-FVVEHDFIMATYLADRVIVFD 536
Cdd:cd03224 170 EIFEAIReLRDEGVTiLLVEQNARFALEIADRAYVLE 206
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
373-536 |
1.64e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.61 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVpvlnvsykpqkispkstgsvrqllhekirdaYTHPQFVTDVMKPLQIE 452
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------------YIDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 453 NIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQR-----LMAARVVKRFILHAKKTAFVVEHDFIM--- 524
Cdd:smart00382 52 IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLLLLLKSEKNLTVILTTNDEKDlgp 131
|
170
....*....|....
gi 108773782 525 --ATYLADRVIVFD 536
Cdd:smart00382 132 alLRRRFDRRIVLL 145
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
101-276 |
1.73e-09 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 57.05 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEIltYFRGSELQNYFTKileDDLKAIIkpqyvdqipkaa 180
Cdd:cd03216 24 RRGEVHALLGENGAGKSTLMKILSGLYKPDSG---------EI--LVDGKEVSFASPR---DARRAGI------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 kgtvgsildrkdetktqAIVCQqldlthlkernvedLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIR 260
Cdd:cd03216 78 -----------------AMVYQ--------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR 126
|
170
....*....|....*.
gi 108773782 261 SLINPDRYIIVVEHDL 276
Cdd:cd03216 127 RLRAQGVAVIFISHRL 142
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
101-250 |
1.83e-09 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 58.35 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLG--KYDDppdwQEILTYfRGSELQNYFTKI--LEDDLkAIIKPQYVDQ- 175
Cdd:cd03256 25 NPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGsvLIDG----TDINKL-KGKALRQLRRQIgmIFQQF-NLIERLSVLEn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 176 --IPK-AAKGTVGSILDR-KDETKTQAIVC-QQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:cd03256 99 vlSGRlGRRSTWRSLFGLfPKEEKQRALAAlERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPA 178
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
371-541 |
1.88e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 371 DSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEvpvlNVSYKPQKISPKSTGSVRQ--------LLHEKI-RDAY 436
Cdd:PRK10253 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldGE----HIQHYASKEVARRIGLLAQnattpgdiTVQELVaRGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 437 TH-PQF----------VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVK 505
Cdd:PRK10253 108 PHqPLFtrwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 108773782 506 RFILHAKKTAFVVEHDFIMATYLA-------DRVIVFDGVPSK 541
Cdd:PRK10253 188 ELNREKGYTLAAVLHDLNQACRYAshlialrEGKIVAQGAPKE 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
101-535 |
1.92e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLG-------KYD--DPPDWQEILTYFRGSELQnyftkiLEDDLkAIIKPQ 171
Cdd:PRK09700 29 YPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinniNYNklDHKLAAQLGIGIIYQELS------VIDEL-TVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 172 YVDQIPkaAKGTVG-SILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:PRK09700 102 YIGRHL--TKKVCGvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 251 QRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAY----------GVVTMPFSvREGINIFLDGyvpTE 320
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCsgmvsdvsndDIVRLMVG-RELQNRFNAM---KE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 321 NLRFRDASLVFkvaetaneeEVKKMCMYKypgmKKKMGEFELAIVAGeftdsEIMVMLGENGTGKTTFIRMLAGrLKPDE 400
Cdd:PRK09700 256 NVSNLAHETVF---------EVRNVTSRD----RKKVRDISFSVCRG-----EILGFAGLVGSGRTELMNCLFG-VDKRA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 401 GGEVpVLNvsykPQKISPKS------------------TG-----SVRQ------------------LLHEKIRDAYTHP 439
Cdd:PRK09700 317 GGEI-RLN----GKDISPRSpldavkkgmayitesrrdNGffpnfSIAQnmaisrslkdggykgamgLFHEVDEQRTAEN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 440 QfvtdvMKPLQIE-NIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVkRFILHAKKTAFVV 518
Cdd:PRK09700 392 Q-----RELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM-RQLADDGKVILMV 465
|
490
....*....|....*....
gi 108773782 519 EHDF--IMAtyLADRVIVF 535
Cdd:PRK09700 466 SSELpeIIT--VCDRIAVF 482
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
354-551 |
2.01e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 59.39 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 354 KKKMGEFELAI-VAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVPVLNVSykPQ------------- 414
Cdd:COG1118 9 SKRFGSFTLLDdVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGrivlnGRDLFTNLP--PRerrvgfvfqhyal 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 415 --------------KISPKSTGSVRQLLHEKIrdaythpqfvtdvmKPLQIENIIDQEVQTLSGGELQRVALALCLGKPA 480
Cdd:COG1118 87 fphmtvaeniafglRVRPPSKAEIRARVEELL--------------ELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 481 DVYLIDEP-SAyLDS----EQRlmaaRVVKRfiLHAK--KTAFVVEHDFIMATYLADRVIVFDG-----VPSKNTVANSP 548
Cdd:COG1118 153 EVLLLDEPfGA-LDAkvrkELR----RWLRR--LHDElgGTTVFVTHDQEEALELADRVVVMNQgrieqVGTPDEVYDRP 225
|
...
gi 108773782 549 QTL 551
Cdd:COG1118 226 ATP 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
103-252 |
2.04e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.85 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKY--------DDPPDWQEILTYFRGSELQNYFTkiLEDDLKAIIKPqyvD 174
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQRPINMMFQSYALFPHMT--VEQNIAFGLKQ---D 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 QIPKAakgtvgSILDRkdetktqaiVCQQLDLTHLKE---RNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQ 251
Cdd:PRK11607 120 KLPKA------EIASR---------VNEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
.
gi 108773782 252 R 252
Cdd:PRK11607 185 R 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
368-537 |
2.21e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EFTDSEIMVMLGENGTGKTTFIRMLAGRLK--PDEG-GEVPVLNvsykpqkISPKSTgsvrqllhekIRDAYTHPQFVTD 444
Cdd:COG2401 52 EIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGcVDVPDNQ-------FGREAS----------LIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 445 VMKPLQIENIID-----QEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVE 519
Cdd:COG2401 115 AVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVAT 194
|
170
....*....|....*...
gi 108773782 520 HDFIMATYLADRVIVFDG 537
Cdd:COG2401 195 HHYDVIDDLQPDLLIFVG 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
377-552 |
2.34e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.46 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 377 MLGENGTGKTTFIRMLAGRLKPDEgGEVPVLNVSYKPQ-KISPKSTGSVRQL--------LHEKI----RDAYTHPQFVT 443
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDA-GKITVLGVPVPARaRLARARIGVVPQFdnldleftVRENLlvfgRYFGMSTREIE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 444 DVMKPL----QIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQR-LMAARVvkRFILHAKKTAFVV 518
Cdd:PRK13536 151 AVIPSLlefaRLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARhLIWERL--RSLLARGKTILLT 228
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 519 EHDFIMATYLADRVIVFDGvpSKNTVANSPQTLL 552
Cdd:PRK13536 229 THFMEEAERLCDRLCVLEA--GRKIAEGRPHALI 260
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
353-505 |
2.58e-09 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 57.18 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 353 MKKKMGEFELAI---VAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDE-GGEVPVLNVSYKPQKISpKSTGSVRQll 428
Cdd:cd03213 13 VKSSPSKSGKQLlknVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvSGEVLINGRPLDKRSFR-KIIGYVPQ-- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 429 hekirDAYTHPQFVtdVMKPLQIEniidQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSeqrLMAARVVK 505
Cdd:cd03213 90 -----DDILHPTLT--VRETLMFA----AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS---SSALQVMS 152
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
360-533 |
2.90e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 57.83 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 360 FELAivAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG--------GEVPVLNVSykPQKISP--KST-GSVRQLL 428
Cdd:COG4778 32 FSVA--AGECV-----ALTGPSGAGKSTLLKCIYGNYLPDSGsilvrhdgGWVDLAQAS--PREILAlrRRTiGYVSQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 429 HEKIRdaythpqfVT--D-VMKPLqIENIIDQEV-----------------------QTLSGGELQRVALALCLGKPADV 482
Cdd:COG4778 103 RVIPR--------VSalDvVAEPL-LERGVDREEarararellarlnlperlwdlppATFSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 483 YLIDEPSAYLDSEQRlmaaRVVKRFILHAKK--TAFV-VEHDF-IMATyLADRVI 533
Cdd:COG4778 174 LLLDEPTASLDAANR----AVVVELIEEAKArgTAIIgIFHDEeVREA-VADRVV 223
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
157-286 |
3.48e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.56 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 157 TKILEDDLKAIIKPQYVDQIPKAAKGTVGSIldrkdeTKTQAIVcqQLDLTHLK-ERNVEDLSGGELQRFACAVVCIQ-- 233
Cdd:cd03238 35 STLVNEGLYASGKARLISFLPKFSRNKLIFI------DQLQFLI--DVGLGYLTlGQKLSTLSGGELQRVKLASELFSep 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 108773782 234 KADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYlSDFI 286
Cdd:cd03238 107 PGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
361-542 |
3.55e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 57.48 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 361 ELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEGGevpvlnVSYKPQKISpkSTGSVRQLLHEK--------I 432
Cdd:TIGR01184 5 NLTIQQGEF-----ISLIGHSGCGKSTLLNLISGLAQPTSGG------VILEGKQIT--EPGPDRMVVFQNysllpwltV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 433 RD--AYTHPQFVTDVMKPLQiENIIDQEVQ-------------TLSGGELQRVALALCLGKPADVYLIDEPSAYLDS--- 494
Cdd:TIGR01184 72 REniALAVDRVLPDLSKSER-RAIVEEHIAlvglteaadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltr 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 108773782 495 ---EQRLMaarvvkRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKN 542
Cdd:TIGR01184 151 gnlQEELM------QIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAAN 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
377-495 |
3.93e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 377 MLGENGTGKTTFIRMLAGRLKPDEGgEV---PVLNVSYKPQ--KISPKST---------GSVRQLLHE--KIRDAYTHPQ 440
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG-EArpaPGIKVGYLPQepQLDPEKTvrenveegvAEVKAALDRfnEIYAAYAEPD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 441 FVTDV----MKPLQ----------IENII------------DQEVQTLSGGELQRVALA-LCLGKPaDVYLIDEPSAYLD 493
Cdd:PRK11819 117 ADFDAlaaeQGELQeiidaadawdLDSQLeiamdalrcppwDAKVTKLSGGERRRVALCrLLLEKP-DMLLLDEPTNHLD 195
|
..
gi 108773782 494 SE 495
Cdd:PRK11819 196 AE 197
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
364-551 |
4.18e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.84 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 364 IVAGEFTDseimvMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRQllHEKIrdAYTHP--QF 441
Cdd:PRK13648 32 IPKGQWTS-----IVGHNGSGKSTIAKLMIGIEKVKSG------EIFYNNQAITDDNFEKLRK--HIGI--VFQNPdnQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 442 V--------------------------TDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSE 495
Cdd:PRK13648 97 VgsivkydvafglenhavpydemhrrvSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 496 QRLMAARVVKRFILHAKKTAFVVEHDFIMATYlADRVIVFDgvpsKNTV--ANSPQTL 551
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMN----KGTVykEGTPTEI 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
378-537 |
4.40e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.40 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 378 LGENGTGKTTFIRMLAGRLKPDEG-----GEV-PVLNVsykpqkispkSTG-----SVRQ----------LLHEKIRDAY 436
Cdd:COG1134 58 IGRNGAGKSTLLKLIAGILEPTSGrvevnGRVsALLEL----------GAGfhpelTGREniylngrllgLSRKEIDEKF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 437 thpQFVTDVMkplQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAkKTAF 516
Cdd:COG1134 128 ---DEIVEFA---ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESG-RTVI 200
|
170 180
....*....|....*....|.
gi 108773782 517 VVEHDFIMATYLADRVIVFDG 537
Cdd:COG1134 201 FVSHSMGAVRRLCDRAIWLEK 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
373-537 |
4.71e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTG--------------------SVRQ---LLH 429
Cdd:COG1129 31 EVHALLGENGAGKSTLMKILSGVYQPDSG------EILLDGEPVRFRSPRdaqaagiaiihqelnlvpnlSVAEnifLGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 430 EK-----IRDAYTHPQfVTDVMKPLQIEniID--QEVQTLSGGELQRVALALCLGKPADVyLI-DEPSAYLDSE--QRLM 499
Cdd:COG1129 105 EPrrgglIDWRAMRRR-ARELLARLGLD--IDpdTPVGDLSVAQQQLVEIARALSRDARV-LIlDEPTASLTERevERLF 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 108773782 500 aaRVVKRfiLHAKKTAFV-VEHDF--IMAtyLADRVIVF-DG 537
Cdd:COG1129 181 --RIIRR--LKAQGVAIIyISHRLdeVFE--IADRVTVLrDG 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
365-537 |
5.44e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 365 VAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRQLLHEKIRDAYT--H--PQ 440
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSG------DVIFNGQPMSKLSSAAKAELRNQKLGFIYQfhHllPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 441 F--VTDVMKPLQIENIIDQEVQT---------------------LSGGELQRVALALCLGKPADVYLIDEPSAYLDseQR 497
Cdd:PRK11629 102 FtaLENVAMPLLIGKKKPAEINSralemlaavglehranhrpseLSGGERQRVAIARALVNNPRLVLADEPTGNLD--AR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 108773782 498 lmAARVVKRFI--LHAKK-TAF-VVEHDFIMATYLADRVIVFDG 537
Cdd:PRK11629 180 --NADSIFQLLgeLNRLQgTAFlVVTHDLQLAKRMSRQLEMRDG 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
84-304 |
5.51e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 84 THRYCANAFKLHRLPIPRpGEVLGLVGTNGIGKSTALKILAGKQKPN------LGKYDDPPDWQEILTYFRGSELQNYFT 157
Cdd:PRK15056 15 TWRNGHTALRDASFTVPG-GSIAALVGVNGSGKSTLFKALMGFVRLAsgkisiLGQPTRQALQKNLVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 158 KILEDDLkaIIKPQYvdqipkaakGTVGSIldRKDETKTQAIVCQQL---DLTHLKERNVEDLSGGELQRFACAVVCIQK 234
Cdd:PRK15056 94 PVLVEDV--VMMGRY---------GHMGWL--RRAKKRDRQIVTAALarvDMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 235 ADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFS 304
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFT 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
373-509 |
5.90e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.81 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEgGEVPVLNVSYKPQKIS------------PKSTgsVR-QL-----LH----E 430
Cdd:COG4152 28 EIFGLLGPNGAGKTTTIRIILGILAPDS-GEVLWDGEPLDPEDRRrigylpeerglyPKMK--VGeQLvylarLKglskA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 431 KIRDAythpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCL-GKPaDVYLIDEPSAYLDSeqrlMAARVVKRFIL 509
Cdd:COG4152 105 EAKRR------ADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALlHDP-ELLILDEPFSGLDP----VNVELLKDVIR 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
371-533 |
6.00e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 371 DSEIMVMLGENGTGKTTFIRMLaGRLKPDEGGEVPVLNVSYK-PQKISPKSTGSVRQ--------------------LLH 429
Cdd:PRK11124 27 QGETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNHFDfSKTPSDKAIRELRRnvgmvfqqynlwphltvqqnLIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 430 EKIRDA-YTHPQFVTDVMK---PLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEqrlMAARVVK 505
Cdd:PRK11124 106 APCRVLgLSKDQALARAEKlleRLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE---ITAQIVS 182
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 506 rfILH----AKKTAFVVEHDFIMATYLADRVI 533
Cdd:PRK11124 183 --IIRelaeTGITQVIVTHEVEVARKTASRVV 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
362-537 |
6.07e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 56.32 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLN-VSYKPQK--ISpksTGSVRQ--LLHEKIRday 436
Cdd:cd03250 26 LEVPKGELV-----AIVGPVGSGKSSLLSALLGELEKLSG-SVSVPGsIAYVSQEpwIQ---NGTIREniLFGKPFD--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 437 thPQFVTDVMKPLQIENIIDQ-------EVQ----TLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEqrlMAARVVK 505
Cdd:cd03250 94 --EERYEKVIKACALEPDLEIlpdgdltEIGekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH---VGRHIFE 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 108773782 506 RFILHA---KKTAFVVEH--DFIMAtylADRVIVFDG 537
Cdd:cd03250 169 NCILGLllnNKTRILVTHqlQLLPH---ADQIVVLDN 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
377-589 |
6.45e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 377 MLGENGTGKTTFIRMLAGRLKPDEGG-EVPVLNVSYKPQK--ISP--KSTGSV-----RQLLHEKI-RDAYTHPQ-FVTD 444
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTvTVDDITITHKTKDkyIRPvrKRIGMVfqfpeSQLFEDTVeREIIFGPKnFKMN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 445 VMK------PLQIE-----NIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKK 513
Cdd:PRK13646 118 LDEvknyahRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENK 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 514 TAFVVEHDFIMATYLADRVIVFDgvpsKNTVAN--SPQTLLAGMNKfLSQLEITFrrdpnnyrPRINKLNsiKDVEQK 589
Cdd:PRK13646 198 TIILVSHDMNEVARYADEVIVMK----EGSIVSqtSPKELFKDKKK-LADWHIGL--------PEIVQLQ--YDFEQK 260
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
102-497 |
6.97e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDW------QEI-------LTY-------FRG--SELQNYFTKi 159
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWqlawvnQETpalpqpaLEYvidgdreYRQleAQLHDANER- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 160 leDDLKAIikpqyvdqipkaakGTVGSILDRKDETKTQAIVCQQLDLTHLK----ERNVEDLSGGELQRFACAVVCIQKA 235
Cdd:PRK10636 105 --NDGHAI--------------ATIHGKLDAIDAWTIRSRAASLLHGLGFSneqlERPVSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 236 DIFMFDEPSSYLDvkqrLKAAITI-RSLINPDRYIIVVEHDLSVLDYLSDFICCLYgvpsaygvvtmpfsvREGINIFLD 314
Cdd:PRK10636 169 DLLLLDEPTNHLD----LDAVIWLeKWLKSYQGTLILISHDRDFLDPIVDKIIHIE---------------QQSLFEYTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 315 GYVPTEnlRFRDASLVFKVAETANEEE-VKKMCMY-----------KYPGMKKKMGE-------------FELAIVAGEF 369
Cdd:PRK10636 230 NYSSFE--VQRATRLAQQQAMYESQQErVAHLQSYidrfrakatkaKQAQSRIKMLErmeliapahvdnpFHFSFRAPES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 370 TDSEIMVM----------------------------LGENGTGKTTFIRMLAGRLKPDEG--GEVPVLNVSYKPQ----- 414
Cdd:PRK10636 308 LPNPLLKMekvsagygdriildsiklnlvpgsriglLGRNGAGKSTLIKLLAGELAPVSGeiGLAKGIKLGYFAQhqlef 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 415 ------------KISPKSTgsvrqllHEKIRDAYTHPQFVTDVmkplqieniIDQEVQTLSGGELQRVALALCLGKPADV 482
Cdd:PRK10636 388 lradesplqhlaRLAPQEL-------EQKLRDYLGGFGFQGDK---------VTEETRRFSGGEKARLVLALIVWQRPNL 451
|
490
....*....|....*
gi 108773782 483 YLIDEPSAYLDSEQR 497
Cdd:PRK10636 452 LLLDEPTNHLDLDMR 466
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
362-537 |
7.27e-09 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 58.61 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEftdseIMVMLGENGTGKTTFIRMLAG---------RL--------KPDEGGEvpvlNVSYKPQKIS--PkstG 422
Cdd:COG4618 353 FSLEPGE-----VLGVIGPSGSGKSTLARLLVGvwpptagsvRLdgadlsqwDREELGR----HIGYLPQDVElfD---G 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 423 SVR------------------QL--LHEKI---RDAYthpqfvtdvmkplqiENIIDQEVQTLSGGELQRVALALCL-GK 478
Cdd:COG4618 421 TIAeniarfgdadpekvvaaaKLagVHEMIlrlPDGY---------------DTRIGEGGARLSGGQRQRIGLARALyGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 479 PADVYLiDEPSAYLDS--EQRLMAArvvkrfILHAKK---TAFVVEHDF-IMAtyLADRVIVFDG 537
Cdd:COG4618 486 PRLVVL-DEPNSNLDDegEAALAAA------IRALKArgaTVVVITHRPsLLA--AVDKLLVLRD 541
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
103-277 |
8.17e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeilTYFRGSELQNYFTKILEDDLKAIIK----PQYVDQIPK 178
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH-----------VWLDGEHIQHYASKEVARRIGLLAQnattPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 179 AAKGTVGS----ILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLK 254
Cdd:PRK10253 102 VARGRYPHqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180
....*....|....*....|....
gi 108773782 255 AAITIRSLINPDRYII-VVEHDLS 277
Cdd:PRK10253 182 LLELLSELNREKGYTLaAVLHDLN 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
352-533 |
8.53e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.61 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 352 GMKKKMGE------FELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVS------YKPQK 415
Cdd:PRK11247 17 AVSKRYGErtvlnqLDLHIPAGQF-----VAVVGRSGCGKSTLLRLLAGLETPSAGellaGTAPLAEARedtrlmFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 416 ISP--KSTGSVRQLLHEKIRDAythpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD 493
Cdd:PRK11247 92 LLPwkKVIDNVGLGLKGQWRDA------ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 494 SEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVI 533
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
348-537 |
8.73e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.30 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKkmgEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDeGGEVPVLNVSYKPQKIS--PKSTG--- 422
Cdd:COG3840 9 YRYGDFPL---RFDLTIAAGERV-----AILGPSGAGKSTLLNLIAGFLPPD-SGRILWNGQDLTALPPAerPVSMLfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 423 -------SVRQ---L-LHEKIRdaYTHPQF--VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCL--GKPadVYLIDE 487
Cdd:COG3840 80 nnlfphlTVAQnigLgLRPGLK--LTAEQRaqVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLvrKRP--ILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 108773782 488 PSAYLDSEQRL-MAARVVKrfiLHAKK--TAFVVEHDFIMATYLADRVI-VFDG 537
Cdd:COG3840 156 PFSALDPALRQeMLDLVDE---LCRERglTVLMVTHDPEDAARIADRVLlVADG 206
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
7-73 |
8.75e-09 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 52.04 E-value: 8.75e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 7 RIAIVNHDKCKpkKCRQeCKKSCP--VVRMGKlcievtpqSKIAWISETLCIGCGICIKKCPFGALSIV 73
Cdd:COG1149 4 KIPVIDEEKCI--GCGL-CVEVCPegAIKLDD--------GGAPVVDPDLCTGCGACVGVCPTGAITLE 61
|
|
| RLI |
pfam04068 |
Possible Fer4-like domain in RNase L inhibitor, RLI; Possible metal-binding domain in ... |
6-37 |
8.82e-09 |
|
Possible Fer4-like domain in RNase L inhibitor, RLI; Possible metal-binding domain in endoribonuclease RNase L inhibitor. Found at the N-terminal end of RNase L inhibitor proteins, adjacent to the 4Fe-4S binding domain, fer4, pfam00037. Also often found adjacent to the DUF367 domain pfam04034 in uncharacterized proteins. The RNase L system plays a major role in the anti-viral and anti-proliferative activities of interferons, and could possibly play a more general role in the regulation of RNA stability in mammalian cells. Inhibitory activity requires concentration-dependent association of RLI with RNase L.
Pssm-ID: 427689 [Multi-domain] Cd Length: 35 Bit Score: 50.97 E-value: 8.82e-09
10 20 30
....*....|....*....|....*....|....*
gi 108773782 6 TRIAIVNHDKCKPKKCRQ-ECKKSCPV--VRMGKL 37
Cdd:pfam04068 1 MRLAIVDFDQCDPKKCTGrKCIRFCPVreVRTGKK 35
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
6-73 |
8.83e-09 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 52.75 E-value: 8.83e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 6 TRIAIVNHDKCKpkKCRQeCKKSCPVvrmgkLCIEVTPqSKIAWISETLCIGCGICIKKCPFGALSIV 73
Cdd:COG1144 22 VERPVVDEDKCI--GCGL-CWIVCPD-----GAIRVDD-GKYYGIDYDYCKGCGICAEVCPVKAIEMV 80
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
101-280 |
9.04e-09 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 56.06 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLG--KYDDPPDWQeiltyfrgselqnyftkILEDDLKAIIKpqYVDQIPK 178
Cdd:cd03245 28 RAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsvLLDGTDIRQ-----------------LDPADLRRNIG--YVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 179 AAKGTVGS-ILDRKDETKTQAIV-------CQQLDLTH-------LKERNVEdLSGGELQRFACAVVCIQKADIFMFDEP 243
Cdd:cd03245 89 LFYGTLRDnITLGAPLADDERILraaelagVTDFVNKHpngldlqIGERGRG-LSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 108773782 244 SSYLD------VKQRLKAAItirslinPDRYIIVVEHDLSVLD 280
Cdd:cd03245 168 TSAMDmnseerLKERLRQLL-------GDKTLIIITHRPSLLD 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
353-536 |
9.71e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.58 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 353 MKKKMGEFELAIVAgEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGgEVpVLN----------VSYKPQKispKSTG 422
Cdd:PRK11144 6 FKQQLGDLCLTVNL-TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKG-RI-VLNgrvlfdaekgICLPPEK---RRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 423 SVRQ---LL-HEKIR-------DAYTHPQFvTDVMKPLQIENIIDQEVQTLSGGELQRVAL--ALcLGKPaDVYLIDEPS 489
Cdd:PRK11144 80 YVFQdarLFpHYKVRgnlrygmAKSMVAQF-DKIVALLGIEPLLDRYPGSLSGGEKQRVAIgrAL-LTAP-ELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 108773782 490 AYLD--SEQRLMA-----ARVVKRFILHakktafvVEH--DFIMatYLADRVIVFD 536
Cdd:PRK11144 157 ASLDlpRKRELLPylerlAREINIPILY-------VSHslDEIL--RLADRVVVLE 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
348-495 |
9.91e-09 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 58.14 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDeGGEVPVLNVSykpqkISPKSTGSVRQL 427
Cdd:TIGR02868 342 AGYPGAPPVLDGVSLDLPPGERV-----AILGPSGSGKSTLLATLAGLLDPL-QGEVTLDGVP-----VSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 428 LHEKIRDAYThpqFVTDVMKPLQI--ENIIDQEV----------------------------QTLSGGELQRVALALCLG 477
Cdd:TIGR02868 411 VSVCAQDAHL---FDTTVRENLRLarPDATDEELwaalervgladwlralpdgldtvlgeggARLSGGERQRLALARALL 487
|
170
....*....|....*...
gi 108773782 478 KPADVYLIDEPSAYLDSE 495
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAE 505
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
373-501 |
1.28e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.19 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRQLLH-------EKIRDAYTHPQFVTDV 445
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAG------RVLLNGGPLDFQRDSIARGLLYlghapgiKTTLSVLENLRFWHAD 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 446 MKPLQIENIIDQ---------EVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD--SEQRLMAA 501
Cdd:cd03231 101 HSDEQVEEALARvglngfedrPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkaGVARFAEA 167
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
97-262 |
1.43e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.04 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 97 LPIPRpGEVLGLVGTNGIGKSTALKILAGKQKPNLGK-YDDPPD-------WQEILTYFrgselQNY--FTKI-LEDDLK 165
Cdd:PRK11432 27 LTIKQ-GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQiFIDGEDvthrsiqQRDICMVF-----QSYalFPHMsLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 166 AIIKPQyvdQIPKAakgtvgsilDRKDETKTQ-AIVcqqlDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPS 244
Cdd:PRK11432 101 YGLKML---GVPKE---------ERKQRVKEAlELV----DLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170
....*....|....*...
gi 108773782 245 SYLDVKQRLKAAITIRSL 262
Cdd:PRK11432 165 SNLDANLRRSMREKIREL 182
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
368-535 |
1.56e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.17 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGevpVLnVSYKPQKISPKSTGSVRQLLHEKIRDA-----YTH---- 438
Cdd:PRK13638 23 DFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA---VL-WQGKPLDYSKRGLLALRQQVATVFQDPeqqifYTDidsd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 439 ---------------PQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARV 503
Cdd:PRK13638 99 iafslrnlgvpeaeiTRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 504 VKRFILHAKKTAfVVEHDFIMATYLADRVIVF 535
Cdd:PRK13638 179 IRRIVAQGNHVI-ISSHDIDLIYEISDAVYVL 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
102-495 |
1.56e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGK----------Y--DDPP----------------DWQEILTYF-----R 148
Cdd:PRK11819 32 PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpapgikvgYlpQEPQldpektvrenveegvaEVKAALDRFneiyaA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 149 GSELQNYFTKILED--DLKAIIkpqyvdqipkAAKGtvGSILDRKDETKTQAIVCQQLDLthlkerNVEDLSGGELQRFA 226
Cdd:PRK11819 112 YAEPDADFDALAAEqgELQEII----------DAAD--AWDLDSQLEIAMDALRCPPWDA------KVTKLSGGERRRVA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 227 CAVVCIQKADIFMFDEPSSYLD------VKQRLKaaitirslinpdRY---IIVVEHDLSVLDYLSDFICCL---YGVP- 293
Cdd:PRK11819 174 LCRLLLEKPDMLLLDEPTNHLDaesvawLEQFLH------------DYpgtVVAVTHDRYFLDNVAGWILELdrgRGIPw 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 294 ----SAYgvvtmpfsvreginifldgyvptenlrfrdasLVFKVAETANEE--EVK-----------------------K 344
Cdd:PRK11819 242 egnySSW--------------------------------LEQKAKRLAQEEkqEAArqkalkrelewvrqspkarqaksK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 345 MCMYKYPGM-----KKKMGEFELAIVAGE---------------FTD-------------SEIMVMLGENGTGKTTFIRM 391
Cdd:PRK11819 290 ARLARYEELlseeyQKRNETNEIFIPPGPrlgdkvieaenlsksFGDrlliddlsfslppGGIVGIIGPNGAGKSTLFKM 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 392 LAGRLKPDeGGEVPV---LNVSYKPQ---KISPKSTgsvrqlLHEKIRDAythpqfvTDVMKPLQIE----------NII 455
Cdd:PRK11819 370 ITGQEQPD-SGTIKIgetVKLAYVDQsrdALDPNKT------VWEEISGG-------LDIIKVGNREipsrayvgrfNFK 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 108773782 456 --DQE--VQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSE 495
Cdd:PRK11819 436 ggDQQkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
366-533 |
1.66e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.49 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 366 AGEFTdseimVMLGENGTGKTTFIRMLAGRLKPD------EGGEVPVLN-------VSYKPQkiSPKSTG-SVRQ--LLH 429
Cdd:PRK10247 32 AGEFK-----LITGPSGCGKSTLLKIVASLISPTsgtllfEGEDISTLKpeiyrqqVSYCAQ--TPTLFGdTVYDnlIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 430 EKIRDAYTHPQ-FVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFI 508
Cdd:PRK10247 105 WQIRNQQPDPAiFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYV 184
|
170 180
....*....|....*....|....*
gi 108773782 509 LHAKKTAFVVEHDFIMATYlADRVI 533
Cdd:PRK10247 185 REQNIAVLWVTHDKDEINH-ADKVI 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
347-541 |
1.78e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.21 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 347 MYKYPGMKKKMGEFELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSYKPQKIS----PKSTG 422
Cdd:PRK13637 13 MEGTPFEKKALDNVNIEIEDGEF-----VGLIGHTGSGKSTLIQHLNGLLKPTSG-KIIIDGVDITDKKVKlsdiRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 423 SV-----RQLLHEKI-RDAYTHPQ-----------FVTDVMK--PLQIENIIDQEVQTLSGGELQRVALALCLGKPADVY 483
Cdd:PRK13637 87 LVfqypeYQLFEETIeKDIAFGPInlglseeeienRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 484 LIDEPSAYLDSEQRLMAARVVKRfiLHAKK--TAFVVEHDFIMATYLADRVIV-------FDGVPSK 541
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKE--LHKEYnmTIILVSHSMEDVAKLADRIIVmnkgkceLQGTPRE 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
101-290 |
1.83e-08 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 55.20 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK-YDDPPDWQEiltyFRGSELQNYFTKI--------LEDDLkaiikpq 171
Cdd:cd03261 24 RRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvLIDGEDISG----LSEAELYRLRRRMgmlfqsgaLFDSL------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 172 yvdqipkaakgtvgSILD----------RKDETKTQAIVCQQLD---LTHLKERNVEDLSGGELQRFACAVVCIQKADIF 238
Cdd:cd03261 93 --------------TVFEnvafplrehtRLSEEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 239 MFDEPSSYLD-----VKQRLkaaitIRSLinPDRY---IIVVEHDLSVLDYLSDFICCLY 290
Cdd:cd03261 159 LYDEPTAGLDpiasgVIDDL-----IRSL--KKELgltSIMVTHDLDTAFAIADRIAVLY 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
365-553 |
2.66e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 365 VAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGG------EVPVL--------NVSYKPQKISPKSTGSVRQLLHE 430
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddeDISLLplhararrGIGYLPQEASIFRRLSVYDNLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 431 --KIRDAYTHPQF---VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSeqrlMAARVVK 505
Cdd:PRK10895 102 vlQIRDDLSAEQRedrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP----ISVIDIK 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 506 RFILHAKKTA---FVVEHDFIMATYLADRVIVfdgVPSKNTVAN-SPQTLLA 553
Cdd:PRK10895 178 RIIEHLRDSGlgvLITDHNVRETLAVCERAYI---VSQGHLIAHgTPTEILQ 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
101-276 |
2.69e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.23 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAG----------KQKPnLGKYDdPPDwqeiLTYFRGselqnYFTkilEDDLKAIIKP 170
Cdd:COG4138 20 NAGELIHLIGPNGAGKSTLLARMAGllpgqgeillNGRP-LSDWS-AAE----LARHRA-----YLS---QQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 171 --QYVD--QIPKAAKGTVGSILDRkdetktqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQ-------KADIFM 239
Cdd:COG4138 86 vfQYLAlhQPAGASSEAVEQLLAQ---------LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 108773782 240 FDEPSSYLDVKQrlKAAIT--IRSLINPDRYIIVVEHDL 276
Cdd:COG4138 157 LDEPMNSLDVAQ--QAALDrlLRELCQQGITVVMSSHDL 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
375-536 |
2.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.58 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 375 MVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVR------------QLLHEKIR--------- 433
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSG------SVLIRGEPITKENIREVRkfvglvfqnpddQIFSPTVEqdiafgpin 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 434 ---DAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILH 510
Cdd:PRK13652 107 lglDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPET 186
|
170 180
....*....|....*....|....*.
gi 108773782 511 AKKTAFVVEHDFIMATYLADRVIVFD 536
Cdd:PRK13652 187 YGMTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| HycB_like |
cd10554 |
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
7-90 |
2.76e-08 |
|
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.
Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 53.03 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 7 RIAIVNHDK-CKPKKCRQ-E---CKKSCPVvrmGklCIEVTPQSKIawISETLCIGCGICIKKCPFGALSIV-NLPSNLE 80
Cdd:cd10554 41 RLRVVKTGEvTAPVQCRQcEdapCANVCPV---G--AISQEDGVVQ--VDEERCIGCKLCVLACPFGAIEMApTTVPGVD 113
|
90
....*....|
gi 108773782 81 KETTHRYCAN 90
Cdd:cd10554 114 WERGPRAVAV 123
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
372-537 |
2.78e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.46 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 372 SEIMVMLGENGTGKTTFIRMLAGRLKPDeGGEV-----PV--LNVSYK--------------PQKISPKSTgsVRQLLHE 430
Cdd:PRK10419 38 GETVALLGRSGCGKSTLARLLVGLESPS-QGNVswrgePLakLNRAQRkafrrdiqmvfqdsISAVNPRKT--VREIIRE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 431 KIR-----DAYTHPQFVTDVMKPLQI-ENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVV 504
Cdd:PRK10419 115 PLRhllslDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLL 194
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 505 KRfILHAKKTAFV-VEHDFIMATYLADRVIVFDG 537
Cdd:PRK10419 195 KK-LQQQFGTACLfITHDLRLVERFCQRVMVMDN 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
101-287 |
3.36e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 56.35 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY-----DDPPDWQEILTYFRGSELQnyFTKILEDDLKAIIKPQYVDQ 175
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgDEWVDMTKPGPDGRGRAKR--YIGILHQEYDLYPHRTVLDN 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 176 IPKAakgtVGsiLDRKDE-TKTQA-IVCQQLDLTHLKERNVED-----LSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:TIGR03269 386 LTEA----IG--LELPDElARMKAvITLKMVGFDEEKAEEILDkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 249 VKQRLKAAITI-RSLINPDRYIIVVEHDlsvLDYLSDfIC 287
Cdd:TIGR03269 460 PITKVDVTHSIlKAREEMEQTFIIVSHD---MDFVLD-VC 495
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
362-539 |
3.52e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 54.87 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPV-------------------LNV------SYK 412
Cdd:COG4525 28 LTIESGEFV-----VALGASGCGKTTLLNLIAGFLAPSSGeitlDGVPVtgpgadrgvvfqkdallpwLNVldnvafGLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 413 PQKISPKSTgsvRQLLHEKIR-----DAYTHPqfvtdvmkplqieniIDQevqtLSGGELQRVALALCLGKPADVYLIDE 487
Cdd:COG4525 103 LRGVPKAER---RARAEELLAlvglaDFARRR---------------IWQ----LSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 488 PSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVP 539
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGP 212
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
8-78 |
3.56e-08 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 54.73 E-value: 3.56e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 8 IAIVNHDKCKpkKCRQeCKKSCPVvrmgkLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVNLPSN 78
Cdd:COG1145 176 KAVIDAEKCI--GCGL-CVKVCPT-----GAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISLEPKEIE 238
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
362-552 |
3.64e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.71 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEftdseIMVMLGENGTGKTTFIRMLaGRLKPDEGGEVPVLNVSYKpqkiSPKStgSVRQLLHEK---IRDAYTH 438
Cdd:PRK09493 22 LNIDQGE-----VVVIIGPSGSGKSTLLRCI-NKLEEITSGDLIVDGLKVN----DPKV--DERLIRQEAgmvFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 439 PQF--VTDVM-KPLQIENIIDQEVQT---------------------LSGGELQRVALALCLGKPADVYLIDEPSAYLDS 494
Cdd:PRK09493 90 PHLtaLENVMfGPLRVRGASKEEAEKqarellakvglaerahhypseLSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 495 EQRLMAARVVKRFilhAKK--TAFVVEHDFIMATYLADRVIVFDGvpSKNTVANSPQTLL 552
Cdd:PRK09493 170 ELRHEVLKVMQDL---AEEgmTMVIVTHEIGFAEKVASRLIFIDK--GRIAEDGDPQVLI 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-541 |
3.64e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 365 VAGEFTDSEIMVMLGENGTGKTTFIRMLaGRLKPDEG-----GEVPVLNVSYKPQKISPKSTGSVRQLLHEK-------I 432
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESevrveGRVEFFNQNIYERRVNLNRLRRQVSMVHPKpnlfpmsV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 433 RD--AYT------HPQFVTD--VMKPL-------QIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSE 495
Cdd:PRK14258 105 YDnvAYGvkivgwRPKLEIDdiVESALkdadlwdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 108773782 496 QRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSK 541
Cdd:PRK14258 185 ASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
101-280 |
3.88e-08 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 56.31 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYddppdwqeiltYFRGSELQNYftkiLEDDLKAIIKpqYVDQipkaa 180
Cdd:COG4987 359 PPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI-----------TLGGVDLRDL----DEDDLRRRIA--VVPQ----- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 kgTV----GSILD-----RKDETKTQAI-VCQQLDLTHLKERNVEDL-----------SGGELQRFACAVVCIQKADIFM 239
Cdd:COG4987 417 --RPhlfdTTLREnlrlaRPDATDEELWaALERVGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALARALLRDAPILL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 108773782 240 FDEPSSYLDvkqrlkaAITIRSLIN------PDRYIIVVEHDLSVLD 280
Cdd:COG4987 495 LDEPTEGLD-------AATEQALLAdllealAGRTVLLITHRLAGLE 534
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
103-276 |
3.93e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.00 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLG--KYDDPPDWQEILTYFR---GSELQN---YFTKI-LEDDLkaiikpqyv 173
Cdd:PRK13632 35 GEYVAILGHNGSGKSTISKILTGLLKPQSGeiKIDGITISKENLKEIRkkiGIIFQNpdnQFIGAtVEDDI--------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 174 dqipkaAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRL 253
Cdd:PRK13632 106 ------AFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180
....*....|....*....|....
gi 108773782 254 KAAITIRSLINP-DRYIIVVEHDL 276
Cdd:PRK13632 180 EIKKIMVDLRKTrKKTLISITHDM 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
101-279 |
4.60e-08 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 55.76 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELqnyfTKILEDDLKAIIKpqYVDQIPKAA 180
Cdd:TIGR02857 346 PPGERVALVGPSGAGKSTLLNLLLGFVDPTEG---------SIA--VNGVPL----ADADADSWRDQIA--WVPQHPFLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTVGS--ILDRKDETKTQaiVCQQLDLTHLKE--------------RNVEDLSGGELQRFACAVVCIQKADIFMFDEPS 244
Cdd:TIGR02857 409 AGTIAEniRLARPDASDAE--IREALERAGLDEfvaalpqgldtpigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190
....*....|....*....|....*....|....*..
gi 108773782 245 SYLD--VKQRLKAAitIRSLINpDRYIIVVEHDLSVL 279
Cdd:TIGR02857 487 AHLDaeTEAEVLEA--LRALAQ-GRTVLLVTHRLALA 520
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
378-553 |
4.77e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.64 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 378 LGENGTGKTTFIRMLAGRLKPDEG----GEvPVLNVSYKPQKISP--KSTGSV-----RQLLHEKI-RDAYTHPQ-F-VT 443
Cdd:PRK13634 39 IGHTGSGKSTLLQHLNGLLQPTSGtvtiGE-RVITAGKKNKKLKPlrKKVGIVfqfpeHQLFEETVeKDICFGPMnFgVS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 444 D------VMKPLQI----ENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRL----MAARvvkrfiL 509
Cdd:PRK13634 118 EedakqkAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKemmeMFYK------L 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 108773782 510 HAKK--TAFVVEHDFIMATYLADRVIVFDgvpsKNTV--ANSPQTLLA 553
Cdd:PRK13634 192 HKEKglTTVLVTHSMEDAARYADQIVVMH----KGTVflQGTPREIFA 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
103-275 |
4.79e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.42 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKY--------DDPPDWQEILTYFRGSELQNYFTkiLEDDLKAIIKpqyvd 174
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmnDVPPAERGVGMVFQSYALYPHLS--VAENMSFGLK----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 qIPKAAKGtvgSILDRKDEtktqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLK 254
Cdd:PRK11000 102 -LAGAKKE---EINQRVNQ------VAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
170 180
....*....|....*....|..
gi 108773782 255 AAITIRSLINP-DRYIIVVEHD 275
Cdd:PRK11000 172 MRIEISRLHKRlGRTMIYVTHD 193
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
375-536 |
5.19e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 375 MV-MLGENGTGKTTFIRMLAGRLKPDEG-----GE---------------------VPVL----NVSY--KPQKISpkst 421
Cdd:PRK11432 34 MVtLLGPSGCGKTTVLRLVAGLEKPTEGqifidGEdvthrsiqqrdicmvfqsyalFPHMslgeNVGYglKMLGVP---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 422 gsvrqllHEKIRdaythpQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSE-QRLMA 500
Cdd:PRK11432 110 -------KEERK------QRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANlRRSMR 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 108773782 501 ARV---VKRFILhakkTAFVVEHDFIMATYLADRVIVFD 536
Cdd:PRK11432 177 EKIrelQQQFNI----TSLYVTHDQSEAFAVSDTVIVMN 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
103-284 |
5.52e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 54.43 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeilTYFRGSELqnyfTKILEDDLKAIIKP-QYVDQ-IPKA- 179
Cdd:TIGR02769 37 GETVGLLGRSGCGKSTLARLLLGLEKPAQGT-----------VSFRGQDL----YQLDRKQRRAFRRDvQLVFQdSPSAv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 180 -AKGTVGSI-------LDRKDETKTQAIVCQQLDLTHLK----ERNVEDLSGGELQRfacavVCIQKA-----DIFMFDE 242
Cdd:TIGR02769 102 nPRMTVRQIigeplrhLTSLDESEQKARIAELLDMVGLRsedaDKLPRQLSGGQLQR-----INIARAlavkpKLIVLDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 108773782 243 PSSYLDVKQRLKAAITIRSLinPDRY---IIVVEHDLSVLDYLSD 284
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKL--QQAFgtaYLFITHDLRLVQSFCQ 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
101-488 |
5.60e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELQNYFTKILEDDLKAIIK------PQ--- 171
Cdd:PRK11288 28 RAGQVHALMGENGAGKSTLLKILSGNYQPDAG---------SIL--IDGQEMRFASTTAALAAGVAIIYqelhlvPEmtv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 172 ----YVDQIPkaakgTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYL 247
Cdd:PRK11288 97 aenlYLGQLP-----HKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 248 DVK--QRLKAaiTIRSLINPDRYIIVVEHDLSVLDYLSDficclygvpsaygvvtmpfsvreGINIFLDG-YVPTenlrF 324
Cdd:PRK11288 172 SAReiEQLFR--VIRELRAEGRVILYVSHRMEEIFALCD-----------------------AITVFKDGrYVAT----F 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 325 RDaslvfkVAETANEEEVKKMC------MYKY-----------------PGMKkkmGEFELAIVAGeftdsEIMVMLGEN 381
Cdd:PRK11288 223 DD------MAQVDRDQLVQAMVgreigdIYGYrprplgevrlrldglkgPGLR---EPISFSVRAG-----EIVGLFGLV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 382 GTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTG-----------------------SVRQLLHEKIRDAYTH 438
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAG------QVYLDGKPIDIRSPRdairagimlcpedrkaegiipvhSVADNINISARRHHLR 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 439 PQFVTDVMKP-----LQIE--NI----IDQEVQTLSGGELQRVALALCLGKPADVYLIDEP 488
Cdd:PRK11288 363 AGCLINNRWEaenadRFIRslNIktpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
101-534 |
7.05e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFT----------KILEDDLKAIIKP 170
Cdd:PRK15439 35 HAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVpqepllfpnlSVKENILFGLPKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 171 QYVDQIPKAAKGTVGSILDRKDETKTQAIVCQQLdlthlkernVEDLSGgeLQRfacavvciqKADIFMFDEPSSYLDVK 250
Cdd:PRK15439 115 QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQI---------VEILRG--LMR---------DSRILILDEPTASLTPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 251 QRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFIcclygvpsaygvvtmpfSV-REGInIFLDGyvPTENlrFRDASL 329
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI-----------------SVmRDGT-IALSG--KTAD--LSTDDI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 330 V---FKVAETANEEEVKKMCMyKYPGMKK-KMGEFELAIV---AGE-FTD-------SEIMVMLGENGTGKTTFIRMLAG 394
Cdd:PRK15439 233 IqaiTPAAREKSLSASQKLWL-ELPGNRRqQAAGAPVLTVedlTGEgFRNislevraGEILGLAGVVGAGRTELAETLYG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 395 rLKPDEGGEVpVLNvsykPQKISPKST------GSV-----RQ----LLHEKIR---DAYTH--PQFVTDVMK------- 447
Cdd:PRK15439 312 -LRPARGGRI-MLN----GKEINALSTaqrlarGLVylpedRQssglYLDAPLAwnvCALTHnrRGFWIKPARenavler 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 448 ---PLQIE-NIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRfiLHAKKTAFV-VEHDF 522
Cdd:PRK15439 386 yrrALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS--IAAQNVAVLfISSDL 463
|
490
....*....|..
gi 108773782 523 IMATYLADRVIV 534
Cdd:PRK15439 464 EEIEQMADRVLV 475
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
373-539 |
7.10e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLN------VSYKPQKISPKSTGSVRQLLHEKIRDAYTHPQFV 442
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVESGqiqiDGKTATRgdrsrfMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 443 TDvmKPLQIENIIDQE---VQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFiLHAKKTAFVVE 519
Cdd:PRK13543 118 PG--SALAIVGLAGYEdtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAH-LRGGGAALVTT 194
|
170 180
....*....|....*....|
gi 108773782 520 HDFIMATYLADRVIVFDGVP 539
Cdd:PRK13543 195 HGAYAAPPVRTRMLTLEAAA 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
360-554 |
7.40e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.43 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 360 FELAIVAGEftdseIMVMLGENGTGKTTFIRMLAGRLKPDEGGevpvLNVSYKPQKISPKSTGSVRQL------------ 427
Cdd:PRK10771 18 FDLTVERGE-----RVAILGPSGAGKSTLLNLIAGFLTPASGS----LTLNGQDHTTTPPSRRPVSMLfqennlfshltv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 428 -------LHEKIR-DAYTHPQfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQR-- 497
Cdd:PRK10771 89 aqniglgLNPGLKlNAAQREK-LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRqe 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 498 ----------------LM-------AARVVKRFILhakktafvvehdfimatyLADRVIVFDGvpskntvanSPQTLLAG 554
Cdd:PRK10771 168 mltlvsqvcqerqltlLMvshsledAARIAPRSLV------------------VADGRIAWDG---------PTDELLSG 220
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
9-73 |
7.77e-08 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 51.24 E-value: 7.77e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 9 AIVNHDKCKpkKCRqECKKSCPVvrmGKLCIEVTPQSKIawiSETLCIGCGICIKKCPFGALSIV 73
Cdd:cd10549 73 AEIDEEKCI--GCG-LCVKVCPV---DAITLEDELEIVI---DKEKCIGCGICAEVCPVNAIKLV 128
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
101-289 |
9.87e-08 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK-YDDPPDWQEI-LTYFR---GSELQNyfTKILEDDLKAIIKPQYVD- 174
Cdd:cd03253 25 PAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSiLIDGQDIREVtLDSLRraiGVVPQD--TVLFNDTIGYNIRYGRPDa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 ---QIPKAAKGTV--GSILDRKDETKTQaivcqqldlthLKERNVEdLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:cd03253 103 tdeEVIEAAKAAQihDKIMRFPDGYDTI-----------VGERGLK-LSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 108773782 250 KQRLKAAITIRSLINpDRYIIVVEHDLS-VLDylSDFICCL 289
Cdd:cd03253 171 HTEREIQAALRDVSK-GRTTIVIAHRLStIVN--ADKIIVL 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
97-290 |
1.09e-07 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 52.95 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 97 LPIPrPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddpPDWQEILtyFRGSELQNYFTKILEddLKAIIkpQYVDQI 176
Cdd:cd03260 21 LDIP-KGEITALIGPSGCGKSTLLRLLNRLNDLIPGA----PDEGEVL--LDGKDIYDLDVDVLE--LRRRV--GMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 177 PKAAKGTV------G-SILDRKDETKTQAIVCQQLDLTHLKErNVED------LSGGELQRFACAVVCIQKADIFMFDEP 243
Cdd:cd03260 90 PNPFPGSIydnvayGlRLHGIKLKEELDERVEEALRKAALWD-EVKDrlhalgLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 108773782 244 SSYLDVKQRLKAAITIRSLiNPDRYIIVVEHDLSVLDYLSDFICCLY 290
Cdd:cd03260 169 TSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLL 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
101-290 |
1.09e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.53 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwQEILtyFRGSELQNyftkiLEDDLKA----IIKPQYVDQI 176
Cdd:cd03217 24 KKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTE-------GEIL--FKGEDITD-----LPPEERArlgiFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 177 PkaakG-TVGSILdrkdetktqaivcqqldlthlkeRNV-EDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLK 254
Cdd:cd03217 90 P----GvKNADFL-----------------------RYVnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 108773782 255 AAITIRSLINPDRYIIVVEHDLSVLDYL-SDFICCLY 290
Cdd:cd03217 143 VAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLY 179
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
362-507 |
1.10e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.40 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLkpDEGGEVPVLNVS--------------YKPQKISPKSTGSVRQL 427
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL--PGSGSIQFAGQPleawsaaelarhraYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 428 L----HEKIRDAYTHPQfVTDVMKPLQIENIIDQEVQTLSGGELQRVALA-LCL-----GKP-ADVYLIDEPSAYLDSEQ 496
Cdd:PRK03695 90 LtlhqPDKTRTEAVASA-LNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAaVVLqvwpdINPaGQLLLLDEPMNSLDVAQ 168
|
170
....*....|.
gi 108773782 497 RLMAARVVKRF 507
Cdd:PRK03695 169 QAALDRLLSEL 179
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
101-279 |
1.21e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.45 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY-------DDPPDWQEILTY----FRGSELQnYFTKILEDDLKaiIK 169
Cdd:PRK13644 26 KKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtGDFSKLQGIRKLvgivFQNPETQ-FVGRTVEEDLA--FG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 170 PQYVDQIPKAAKGTVGSILdrkdetktqaivcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:PRK13644 103 PENLCLPPIEIRKRVDRAL-------------AEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190
....*....|....*....|....*....|
gi 108773782 250 KQRLKAAITIRSLINPDRYIIVVEHDLSVL 279
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEEL 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
81-248 |
1.54e-07 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 52.41 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 81 KETTHRYCANAFKLHRLPIPRP-GEVLGLVGTNGIGKSTALKILAGKQKPNLG--KYDDPPdwqeiLTYFRGSELQNYFT 157
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISaGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtiRVNGQD-----VSDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 158 KI--LEDDLKAIIKPQYVDQIPKAAKGTVGSildRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKA 235
Cdd:cd03292 79 KIgvVFQDFRLLPDRNVYENVAFALEVTGVP---PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170
....*....|...
gi 108773782 236 DIFMFDEPSSYLD 248
Cdd:cd03292 156 TILIADEPTGNLD 168
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
456-533 |
1.58e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.26 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 456 DQEVQTLSGGELQRVALALCLGKPAD--VYLIDEPSAYLDSE--QRLMAARVVKRfilHAKKTAFVVEHD--FIMAtylA 529
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRdnDRLIETLKRLR---DLGNTVLVVEHDedTIRA---A 205
|
....
gi 108773782 530 DRVI 533
Cdd:cd03270 206 DHVI 209
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
362-539 |
1.59e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.91 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRL-KPDEGGEVPV-----LN---------------VSYKPQKISPKS 420
Cdd:PRK13547 22 LRIEPGRVT-----ALLGRNGAGKSTLLKALAGDLtGGGAPRGARVtgdvtLNgeplaaidaprlarlRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 421 TGSVRQLL------HEKIRDAYTHP--QFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGK---------PADVY 483
Cdd:PRK13547 97 AFSAREIVllgrypHARRAGALTHRdgEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 484 LIDEPSAYLD--SEQRLMAarVVKRFILHAKKTAFVVEHDFIMATYLADRV-------IVFDGVP 539
Cdd:PRK13547 177 LLDEPTAALDlaHQHRLLD--TVRRLARDWNLGVLAIVHDPNLAARHADRIamladgaIVAHGAP 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
101-290 |
1.65e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.58 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELqnyfTKILEDDLKAI-IKPQYVDQIPKA 179
Cdd:COG4608 42 RRGETLGLVGESGCGKSTLGRLLLRLEEPTSG---------EIL--FDGQDI----TGLSGRELRPLrRRMQMVFQDPYA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 180 A---KGTVGSIL-------DRKDETKTQAIVCQQLDLTHLK----ERNVEDLSGGELQRFACA---------VVCiqkad 236
Cdd:COG4608 107 SlnpRMTVGDIIaeplrihGLASKAERRERVAELLELVGLRpehaDRYPHEFSGGQRQRIGIAralalnpklIVC----- 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 237 ifmfDEPSSYLDV-------------KQRLKAAitirslinpdrYIIvVEHDLSVLDYLSDFICCLY 290
Cdd:COG4608 182 ----DEPVSALDVsiqaqvlnlledlQDELGLT-----------YLF-ISHDLSVVRHISDRVAVMY 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
84-284 |
1.67e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 52.62 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 84 THRY-----CANA-FKLHrlpiprPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDDppdwqeiltyfRGSELQNY 155
Cdd:PRK11701 13 TKLYgprkgCRDVsFDLY------PGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRM-----------RDGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 156 FTkILEDDLKAIIKPQ--YVDQIPK-------AAKGTVGSIL----DRK-DETKTQAIvcQQLDLTHLKERNVEDL---- 217
Cdd:PRK11701 76 YA-LSEAERRRLLRTEwgFVHQHPRdglrmqvSAGGNIGERLmavgARHyGDIRATAG--DWLERVEIDAARIDDLpttf 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 218 SGGELQRFACAVVCIQKAD-IFMfDEPSSYLDVKQRLKAAITIRSLINP-DRYIIVVEHDLSVLDYLSD 284
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRlVFM-DEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAH 220
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
6-74 |
1.68e-07 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 48.51 E-value: 1.68e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 6 TRIAIVNHDKCKpkKCRqECKKSCPVvrmgkLCIevTPQSKIAWISETLCIGCGICIKKCPFGALSIVN 74
Cdd:COG2221 7 TWPPKIDEEKCI--GCG-LCVAVCPT-----GAI--SLDDGKLVIDEEKCIGCGACIRVCPTGAIKGEK 65
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
341-536 |
1.87e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 341 EVKKMCmYKYPGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVlNVSYKPQKI 416
Cdd:PRK13636 7 KVEELN-YNYSDGTHALKGININIKKGEVT-----AILGGNGAGKSTLFQNLNGILKPSSGrilfDGKPI-DYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 417 SPKSTGSVRQLLHEKIRDA--YTHPQF---------------VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKP 479
Cdd:PRK13636 80 LRESVGMVFQDPDNQLFSAsvYQDVSFgavnlklpedevrkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 480 ADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFD 536
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
372-494 |
1.92e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 372 SEIMVMLGENGTGKTTFIRMLAGRLKPDEG--GEVPVLNVSYKPQKISPKSTGSvrqllhekirdaYTHPQfvtDV-MKP 448
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALANRTEGNVSveGDIHYNGIPYKEFAEKYPGEII------------YVSEE---DVhFPT 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 108773782 449 LQIENIID--------QEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDS 494
Cdd:cd03233 98 LTVRETLDfalrckgnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
378-536 |
2.02e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.17 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 378 LGENGTGKTTFIRMLAGRLKPDeGGEVPVLNvsYKPQKISP---KSTGSV---R-QL-----------LHEKI----RDA 435
Cdd:COG4586 54 IGPNGAGKSTTIKMLTGILVPT-SGEVRVLG--YVPFKRRKefaRRIGVVfgqRsQLwwdlpaidsfrLLKAIyripDAE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 436 YTHP-QFVTDVmkpLQIENIIDQEVQTLSGGelQR----VALALcLGKPADVYLiDEPSAYLDseqrLMAARVVKRFILH 510
Cdd:COG4586 131 YKKRlDELVEL---LDLGELLDTPVRQLSLG--QRmrceLAAAL-LHRPKILFL-DEPTIGLD----VVSKEAIREFLKE 199
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 511 AKK----TAFVVEHDfiMA--TYLADRVIVFD 536
Cdd:COG4586 200 YNRergtTILLTSHD--MDdiEALCDRVIVID 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
373-534 |
2.37e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTgsvrqllhekiRDA--------YTHPQFVtD 444
Cdd:COG3845 32 EIHALLGENGAGKSTLMKILYGLYQPDSG------EILIDGKPVRIRSP-----------RDAialgigmvHQHFMLV-P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 445 VMKPLqiENII---------------------------------DQEVQTLSGGELQRVAL--ALCLGkpADVyLI-DEP 488
Cdd:COG3845 94 NLTVA--ENIVlgleptkggrldrkaararirelserygldvdpDAKVEDLSVGEQQRVEIlkALYRG--ARI-LIlDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 108773782 489 SAYL-DSE-QRLMAarVVKRFIlHAKKTAFVVEHDF--IMAtyLADRVIV 534
Cdd:COG3845 169 TAVLtPQEaDELFE--ILRRLA-AEGKSIIFITHKLreVMA--IADRVTV 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
78-277 |
2.41e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.37 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 78 NLEKETTHRYCANAFKLHrlpIPrPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILTyfrGSE-LQNyf 156
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLH---IP-AGQFVAVVGRSGCGKSTLLRLLAGLETPSAG---------ELLA---GTApLAE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 157 tkiLEDDLKAIIkpQYVDQIP-KAAKGTVGsiLDRKDETKTQAIvcQQLDLTHLKERNVE---DLSGGELQRFACAVVCI 232
Cdd:PRK11247 79 ---AREDTRLMF--QDARLLPwKKVIDNVG--LGLKGQWRDAAL--QALAAVGLADRANEwpaALSGGQKQRVALARALI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 108773782 233 QKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRY-IIVVEHDLS 277
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFtVLLVTHDVS 195
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
101-279 |
2.54e-07 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 51.06 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqeiltyfrgselqnyftKILED--DLKAIIKPQYVDQIpk 178
Cdd:cd03246 26 EPGESLAIIGPSGSGKSTLARLILGLLRPTSG-------------------------RVRLDgaDISQWDPNELGDHV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 179 aakGTV--------GSILDrkdetktqaivcqqldlthlkerNVedLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:cd03246 79 ---GYLpqddelfsGSIAE-----------------------NI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190
....*....|....*....|....*....|.
gi 108773782 251 --QRLKAAitIRSLINPDRYIIVVEHDLSVL 279
Cdd:cd03246 131 geRALNQA--IAALKAAGATRIVIAHRPETL 159
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
339-571 |
2.65e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.11 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 339 EEEVKKMCMYKYPGMKKKMGEFELAIVAGEftdseIMVMLGENGTGKTTFIRMLAGRLKPDEGgevPVLNVSYKPQKISP 418
Cdd:PRK10070 26 EQGLSKEQILEKTGLSLGVKDASLAIEEGE-----IFVIMGLSGSGKSTMVRLLNRLIEPTRG---QVLIDGVDIAKISD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 419 KSTGSVRQ------------LLHEKIRD------------AYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALAL 474
Cdd:PRK10070 98 AELREVRRkkiamvfqsfalMPHMTVLDntafgmelaginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLAR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 475 CLGKPADVYLIDEPSAYLDSEQRL-MAARVVKRFILHAKKTAFvVEHDFIMATYLADRVIVFDG-----VPSKNTVANSP 548
Cdd:PRK10070 178 ALAINPDILLMDEAFSALDPLIRTeMQDELVKLQAKHQRTIVF-ISHDLDEAMRIGDRIAIMQNgevvqVGTPDEILNNP 256
|
250 260 270
....*....|....*....|....*....|
gi 108773782 549 -----QTLLAGMN--KFLSQLEITfRRDPN 571
Cdd:PRK10070 257 andyvRTFFRGVDisQVFSAKDIA-RRTPN 285
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
101-248 |
2.86e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.80 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeilTYFRG---SELQNYFTKILEDDLKAIIKPQYV--DQ 175
Cdd:PRK10908 26 RPGEMAFLTGHSGAGKSTLLKLICGIERPSAGK-----------IWFSGhdiTRLKNREVPFLRRQIGMIFQDHHLlmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 176 -------IPKAAKGTVGSILDRKdetktqaiVCQQLDLTHL--KERNVE-DLSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:PRK10908 95 tvydnvaIPLIIAGASGDDIRRR--------VSAALDKVGLldKAKNFPiQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
...
gi 108773782 246 YLD 248
Cdd:PRK10908 167 NLD 169
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
87-278 |
3.06e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 53.59 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 87 YCANAFKLHRLPIPRpGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELQNYFTKILEddlka 166
Cdd:TIGR01193 485 YGSNILSDISLTIKM-NSKTTIVGMSGSGKSTLAKLLVGFFQARSG---------EIL--LNGFSLKDIDRHTLR----- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 167 iikpQYVDQIPKAAKGTVGSILDR----KDETKTQAIVCQQLDL---------------THLKERNvEDLSGGELQRFAC 227
Cdd:TIGR01193 548 ----QFINYLPQEPYIFSGSILENlllgAKENVSQDEIWAACEIaeikddienmplgyqTELSEEG-SSISGGQKQRIAL 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 228 AVVCIQKADIFMFDEPSSYLDVKQRLKaaiTIRSLIN-PDRYIIVVEHDLSV 278
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKK---IVNNLLNlQDKTIIFVAHRLSV 671
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
14-72 |
3.08e-07 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 47.82 E-value: 3.08e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 14 DKCKpkKCRQeCKKSCPVvrmgkLCIEVTP--QSKIAWISETLCIGCGICIKKCPFGALSI 72
Cdd:COG1143 2 DKCI--GCGL-CVRVCPV-----DAITIEDgePGKVYVIDPDKCIGCGLCVEVCPTGAISM 54
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
103-248 |
3.72e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.55 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKYD---------DPPDWQEILTYFR--GSELQNY-----FTkILEDDLKA 166
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdfsKTPSDKAIRELRRnvGMVFQQYnlwphLT-VQQNLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 167 IIKPQYVDqipkaakgtvgsildrKDETKTQAI-VCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:PRK11124 107 PCRVLGLS----------------KDQALARAEkLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
...
gi 108773782 246 YLD 248
Cdd:PRK11124 171 ALD 173
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
97-289 |
3.76e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 51.62 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 97 LPIPRpGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDDppdwQEILTYfRGSELqnyfTKILeddlkAIIKpqyvd 174
Cdd:COG4604 22 LTIPK-GGITALIGPNGAGKSTLLSMISRLLPPDSGEvlVDG----LDVATT-PSREL----AKRL-----AILR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 QIPK-AAKGTV------------GSILDRKDETK-TQAIvcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMF 240
Cdd:COG4604 82 QENHiNSRLTVrelvafgrfpysKGRLTAEDREIiDEAI--AYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 108773782 241 DEPSSYLDVK---QRLKaaiTIRSLINP-DRYIIVVEHDLSVLDYLSDFICCL 289
Cdd:COG4604 160 DEPLNNLDMKhsvQMMK---LLRRLADElGKTVVIVLHDINFASCYADHIVAM 209
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
360-533 |
3.92e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 360 FELAIVAGEftdsEIMVmLGENGTGKTTFIRMLAGRLKPDEgGEVP---VLNVSYKPQKISPKSTGSV------RQLLHE 430
Cdd:PRK15064 338 LNLLLEAGE----RLAI-IGENGVGKTTLLRTLVGELEPDS-GTVKwseNANIGYYAQDHAYDFENDLtlfdwmSQWRQE 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 431 KIRDaythpQFVTDVM-KPLQIENIIDQEVQTLSGGELQRVALA-LCLGKPaDVYLIDEPSAYLDSE--QRLMAArvVKR 506
Cdd:PRK15064 412 GDDE-----QAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGkLMMQKP-NVLVMDEPTNHMDMEsiESLNMA--LEK 483
|
170 180
....*....|....*....|....*..
gi 108773782 507 FilhaKKTAFVVEHDFIMATYLADRVI 533
Cdd:PRK15064 484 Y----EGTLIFVSHDREFVSSLATRII 506
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
102-250 |
4.35e-07 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 50.82 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQnYFTKI--LEDDLKAIIKPQYVDQIPKA 179
Cdd:TIGR01189 25 AGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIL-YLGHLpgLKPELSALENLHFWAAIHGG 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 180 AKGTVGSILDrkdetktqaivcqQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:TIGR01189 104 AQRTIEDALA-------------AVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
368-536 |
4.36e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.75 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVPVLNVSYKPQKISPKSTGSV-----RQLLHEKI-RDAY 436
Cdd:PRK13641 29 ELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGtitiaGYHITPETGNKNLKKLRKKVSLVfqfpeAQLFENTVlKDVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 437 THPQ---FVTDVMKPLQI---------ENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVV 504
Cdd:PRK13641 109 FGPKnfgFSEDEAKEKALkwlkkvglsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLF 188
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 505 KRFiLHAKKTAFVVEHDFIMATYLADRVIVFD 536
Cdd:PRK13641 189 KDY-QKAGHTVILVTHNMDDVAEYADDVLVLE 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
369-536 |
4.44e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.16 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 369 FTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKSTGSVRQLLH--EKIRDA----------Y 436
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYG------TIQVGDIYIGDKKNNHELITNPysKKIKNFkelrrrvsmvF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 437 THPQ---FVTDVMK-----PLQI---------------------ENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDE 487
Cdd:PRK13631 123 QFPEyqlFKDTIEKdimfgPVALgvkkseakklakfylnkmgldDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 108773782 488 PSAYLD--SEQRLMaarvvkRFILHAK---KTAFVVEHDFIMATYLADRVIVFD 536
Cdd:PRK13631 203 PTAGLDpkGEHEMM------QLILDAKannKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
373-504 |
4.44e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQKiSPKSTGSVRQllhEKIRDAYTHPQFvTDVMKPLQIE 452
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQR-EGRLARDIRK---SRANTGYIFQQF-NLVNRLSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 453 NII--------------------------------------DQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDS 494
Cdd:PRK09984 106 NVLigalgstpfwrtcfswftreqkqralqaltrvgmvhfaHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDP 185
|
170
....*....|
gi 108773782 495 EqrlmAARVV 504
Cdd:PRK09984 186 E----SARIV 191
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
10-74 |
4.73e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 48.93 E-value: 4.73e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 10 IVNHDKCKpkKCRQeCKKSCPV--VRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVN 74
Cdd:cd10549 36 EIDEDKCV--FCGA-CVEVCPTgaIELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAITLED 99
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
373-563 |
5.24e-07 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 50.95 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevPVLNVSYKPQKISP----KSTGSVRQ---LLHEKIRD--AYTHP---- 439
Cdd:cd03252 29 EVVGIVGRSGSGKSTLTKLIQRFYVPENG---RVLVDGHDLALADPawlrRQVGVVLQenvLFNRSIRDniALADPgmsm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 440 -------------QFVTDVmkPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKR 506
Cdd:cd03252 106 ervieaaklagahDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 507 FIlhAKKTAFVVEHDfIMATYLADRVIVFDGvpSKNTVANSPQTLLA--GMNKFLSQLE 563
Cdd:cd03252 184 IC--AGRTVIIIAHR-LSTVKNADRIIVMEK--GRIVEQGSHDELLAenGLYAYLYQLQ 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
91-277 |
6.27e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.29 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 91 AFKLHRLP--IPRpGEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeilTYFRGSEL-QNYFTKILEDDLKAI 167
Cdd:PRK13648 22 SFTLKDVSfnIPK-GQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE-----------IFYNNQAItDDNFEKLRKHIGIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 168 IKP--QYVDQIPK--AAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEP 243
Cdd:PRK13648 90 QNPdnQFVGSIVKydVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 244 SSYLDVKQRLKAAITIRSL-INPDRYIIVVEHDLS 277
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVkSEHNITIISITHDLS 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
92-277 |
6.33e-07 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 50.61 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 92 FKLHRlpiprpGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYD-----DPP-----DWQEILT-----YFRGSELQnyf 156
Cdd:cd03220 43 FEVPR------GERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvrgrvSSLlglggGFNPELTgreniYLNGRLLG--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 157 tkileddlkaiIKPQYVDQipkaakgtvgsildRKDETktqaivcqqLDLTHLKE---RNVEDLSGGELQRFACAVVCIQ 233
Cdd:cd03220 114 -----------LSRKEIDE--------------KIDEI---------IEFSELGDfidLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 108773782 234 KADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLS 277
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
101-276 |
6.37e-07 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 52.36 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY--DDPPDWQeiltyfrgselqnyftkILEDDLKAIIKpqYVDQIPK 178
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtlDGVPVSS-----------------LDQDEVRRRVS--VCAQDAH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 179 AAKGTVGSIL-----DRKDETKTQAIVCQQL-----DLTH-LKERNVED---LSGGELQRFACAVVCIQKADIFMFDEPS 244
Cdd:TIGR02868 420 LFDTTVRENLrlarpDATDEELWAALERVGLadwlrALPDgLDTVLGEGgarLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 245 SYLDVKqrlKAAITIRSLINPD--RYIIVVEHDL 276
Cdd:TIGR02868 500 EHLDAE---TADELLEDLLAALsgRTVVLITHHL 530
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-532 |
6.73e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.07 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 352 GMKKKMGEFE-LAIVAGEFTDSEIMVMLGENGTGKTTFIRMLaGRL-----KPDEGGEV----------PVLNVSYKPQK 415
Cdd:PRK14247 8 DLKVSFGQVEvLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLielypEARVSGEVyldgqdifkmDVIELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 416 I----SPKSTGSV----------------RQLLHEKIRDAYTHPQFVTDVmkplqiENIIDQEVQTLSGGELQRVALALC 475
Cdd:PRK14247 87 VfqipNPIPNLSIfenvalglklnrlvksKKELQERVRWALEKAQLWDEV------KDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 476 LGKPADVYLIDEPSAYLDSEQrlmAARVVKRFI-LHAKKTAFVVEHDFIMATYLADRV 532
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPEN---TAKIESLFLeLKKDMTIVLVTHFPQQAARISDYV 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
101-289 |
6.97e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.88 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDwqeiltyfrgselqnyftkileddlkaiIKPQYVDQ---IP 177
Cdd:PRK09544 28 KPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------------------------LRIGYVPQklyLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 178 KAAKGTVGSILDRKDETKTQAI--VCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLka 255
Cdd:PRK09544 80 TTLPLTVNRFLRLRPGTKKEDIlpALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV-- 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 108773782 256 aiTIRSLINPDRY-----IIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK09544 158 --ALYDLIDQLRReldcaVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
350-535 |
7.00e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 350 YPGMKKKMGEFELaivagEFTDSEIMVMLGENGTGKTTFIRML--AGRLKPdeggEVPVL-NVSYKPQKISPKSTGSVRq 426
Cdd:PRK14239 14 YYNKKKALNSVSL-----DFYPNEITALIGPSGSGKSTLLRSInrMNDLNP----EVTITgSIVYNGHNIYSPRTDTVD- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 lLHEKIRDAYTHPQ-----FVTDVMKPLQIENI-----IDQEVQT---------------------LSGGELQRVALALC 475
Cdd:PRK14239 84 -LRKEIGMVFQQPNpfpmsIYENVVYGLRLKGIkdkqvLDEAVEKslkgasiwdevkdrlhdsalgLSGGQQQRVCIARV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108773782 476 LGKPADVYLIDEPSAYLDSeqrlMAARVVKRFILHAKK--TAFVVEHDFIMATYLADRVIVF 535
Cdd:PRK14239 163 LATSPKIILLDEPTSALDP----ISAGKIEETLLGLKDdyTMLLVTRSMQQASRISDRTGFF 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
103-276 |
7.07e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLG-------KYDDPPDW---QEILTYFRGSELQnYFTKILEDDLkaiikpqy 172
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDGLLEAESGqiiidgdLLTEENVWdirHKIGMVFQNPDNQ-FVGATVEDDV-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 vdqipkaAKGTVGSILDRKD--ETKTQAIvcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:PRK13650 104 -------AFGLENKGIPHEEmkERVNEAL--ELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180
....*....|....*....|....*....
gi 108773782 251 QRLKAAITIRSLinPDRY---IIVVEHDL 276
Cdd:PRK13650 175 GRLELIKTIKGI--RDDYqmtVISITHDL 201
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
102-284 |
7.72e-07 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 51.65 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PG-EVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEIltYFRGSELQnyftkileDDLKAIIKPQ------YVD 174
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAGLTRPDEG---------EI--VLNGRTLF--------DSRKGIFLPPekrrigYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 175 Q----IPKAakgTVGSIL-------DRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEP 243
Cdd:TIGR02142 82 QearlFPHL---SVRGNLrygmkraRPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 108773782 244 SSYLDVK---------QRLKAAITIrslinPdryIIVVEHDLSVLDYLSD 284
Cdd:TIGR02142 159 LAALDDPrkyeilpylERLHAEFGI-----P---ILYVSHSLQEVLRLAD 200
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
101-277 |
8.37e-07 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 50.56 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK-YDDPPDWQEI-LTYFR---GSELQN--YFTKILEDDLKAIIKPQYV 173
Cdd:cd03252 26 KPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvLVDGHDLALAdPAWLRrqvGVVLQEnvLFNRSIRDNIALADPGMSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 174 DQIPKAAKgtvgsildrkdETKTQAIVCQqLDL---THLKERNVeDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:cd03252 106 ERVIEAAK-----------LAGAHDFISE-LPEgydTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180
....*....|....*....|....*....
gi 108773782 251 QRlkaAITIRSL--INPDRYIIVVEHDLS 277
Cdd:cd03252 173 SE---HAIMRNMhdICAGRTVIIIAHRLS 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
103-249 |
8.40e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 49.80 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPdwqEILTYFRGSELQNYFTKILEDDLKAIIKPQYVDQIPKAakg 182
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHA--- 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 183 tvgsilDRKDETKTQAIvcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:cd03231 100 ------DHSDEQVEEAL--ARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
102-489 |
9.81e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPN------LGK---YDDPPDWQEI--------------LT----YFRGSELQN 154
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDagsilyLGKevtFNGPKSSQEAgigiihqelnlipqLTiaenIFLGREFVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 155 YFTKILEDDLKAiikpqyvdqipKAAKgtvgsILDRkdetktqaivcqqLDLTHLKERNVEDLSGGELQRFACAVVCIQK 234
Cdd:PRK10762 109 RFGRIDWKKMYA-----------EADK-----LLAR-------------LNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 235 ADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLdylsdficclygvpsaygvvtmpFSVREGINIFLD 314
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEI-----------------------FEICDDVTVFRD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 315 GyvptenlRFRDASlvfKVAETANEEEVKKMCMYK----YPGMKKKMGEFELAI--VAGE------FT--DSEIMVMLGE 380
Cdd:PRK10762 217 G-------QFIAER---EVADLTEDSLIEMMVGRKledqYPRLDKAPGEVRLKVdnLSGPgvndvsFTlrKGEILGVSGL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 381 NGTGKTTFIRMLAGRLkPDEGGEV-----PVLNVSykPQK--------ISPKSTG----------------SVRQLLHEK 431
Cdd:PRK10762 287 MGAGRTELMKVLYGAL-PRTSGYVtldghEVVTRS--PQDglangivyISEDRKRdglvlgmsvkenmsltALRYFSRAG 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 432 IR-DAYTHPQFVTDVMKPLQIEN-IIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPS 489
Cdd:PRK10762 364 GSlKHADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
46-74 |
9.82e-07 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 46.26 E-value: 9.82e-07
10 20
....*....|....*....|....*....
gi 108773782 46 KIAWISETLCIGCGICIKKCPFGALSIVN 74
Cdd:COG1149 4 KIPVIDEEKCIGCGLCVEVCPEGAIKLDD 32
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
97-275 |
9.96e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 51.24 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 97 LPIPRpGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDdppdwqeiltyFRGSEL--------------QNYftkiled 162
Cdd:PRK10851 23 LDIPS-GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIR-----------FHGTDVsrlhardrkvgfvfQHY------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 163 dlkAIIKPQYV-DQIpkaAKGTvgSILDRKDETKTQAI---VCQQLD---LTHLKERNVEDLSGGELQRFACAVVCIQKA 235
Cdd:PRK10851 84 ---ALFRHMTVfDNI---AFGL--TVLPRRERPNAAAIkakVTQLLEmvqLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 108773782 236 DIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIV-VEHD 275
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVfVTHD 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
97-276 |
1.00e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 50.02 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 97 LPIPRpGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--------YDDPPDWQEILTYFRGSELQnyftkiLEDDLKAI- 167
Cdd:cd03267 42 FTIEK-GEIVGFIGPNGAGKTTTLKILSGLLQPTSGEvrvaglvpWKRRKKFLRRIGVVFGQKTQ------LWWDLPVId 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 168 ----IKPQYvdQIPKAAKGTvgsildRKDEtktqaiVCQQLDLTHLKERNVEDLSGGelQRFACAVVC--IQKADIFMFD 241
Cdd:cd03267 115 sfylLAAIY--DLPPARFKK------RLDE------LSELLDLEELLDTPVRQLSLG--QRMRAEIAAalLHEPEILFLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 242 EPSSYLDVKQRLKaaitIRSLI---NPDR--YIIVVEHDL 276
Cdd:cd03267 179 EPTIGLDVVAQEN----IRNFLkeyNRERgtTVLLTSHYM 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
101-133 |
1.08e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.08 E-value: 1.08e-06
10 20 30
....*....|....*....|....*....|...
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK 133
Cdd:COG1134 50 ERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
103-290 |
1.10e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.86 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELqnyfTKILEDDLKAIIKP-QYVDQIPKAA- 180
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDG---------EVA--WLGKDL----LGMKDDEWRAVRSDiQMIFQDPLASl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 --KGTVGSI-----------LDRKD-ETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSY 246
Cdd:PRK15079 112 npRMTIGEIiaeplrtyhpkLSRQEvKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 108773782 247 LDVKQRLKAAITIRSLINP-DRYIIVVEHDLSVLDYLSDFICCLY 290
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMY 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
373-537 |
1.26e-06 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 49.78 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAgRLKPDEGGEV-------PVLNVSYKPQKISpkSTGSVRQLLHEKIRD--AYTHPQFVT 443
Cdd:cd03248 41 EVTALVGPSGSGKSTVVALLE-NFYQPQGGQVlldgkpiSQYEHKYLHSKVS--LVGQEPVLFARSLQDniAYGLQSCSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 444 DVMKPLQ-----------IENIIDQEV----QTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFi 508
Cdd:cd03248 118 ECVKEAAqkahahsfiseLASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDW- 196
|
170 180
....*....|....*....|....*....
gi 108773782 509 lHAKKTAFVVEHDfIMATYLADRVIVFDG 537
Cdd:cd03248 197 -PERRTVLVIAHR-LSTVERADQILVLDG 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
101-277 |
1.26e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.50 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDdpPDWQEILTYFRGSELQN---------YFTKILEDDLKaIIKPQ 171
Cdd:PRK13657 359 KPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL--IDGTDIRTVTRASLRRNiavvfqdagLFNRSIEDNIR-VGRPD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 172 YVD-QIPKAAKGTVGS-ILDRKDetktqaivcQQLDlTHLKERNvEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:PRK13657 436 ATDeEMRAAAERAQAHdFIERKP---------DGYD-TVVGERG-RQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190
....*....|....*....|....*....|.
gi 108773782 250 --KQRLKAAI-TIRSlinpDRYIIVVEHDLS 277
Cdd:PRK13657 505 etEAKVKAALdELMK----GRTTFIIAHRLS 531
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
361-534 |
1.43e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.09 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 361 ELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GE-VPVLNVSYKPQKISPKSTGSVRQLLHEKIRD 434
Cdd:PRK13642 22 QLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidGElLTAENVWNLRRKIGMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 435 ---------AYTHPQFVTDVMKPLQIENIID---QEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAAR 502
Cdd:PRK13642 102 dvafgmenqGIPREEMIKRVDEALLAVNMLDfktREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 503 VVKRFILHAKKTAFVVEHDFIMATYlADRVIV 534
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHDLDEAAS-SDRILV 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
348-537 |
1.43e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYpgMKKKMGEFELAI--VAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSYKPQK----ISpKST 421
Cdd:PRK13633 12 YKY--ESNEESTEKLALddVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEG-KVYVDGLDTSDEEnlwdIR-NKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 422 GSVRQ-----------------------LLHEKIRDAythpqfVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGK 478
Cdd:PRK13633 88 GMVFQnpdnqivativeedvafgpenlgIPPEEIRER------VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 479 PADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHdFIMATYLADRVIVFDG 537
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH-YMEEAVEADRIIVMDS 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
101-293 |
1.47e-06 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 49.39 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyfrgselqnYFTKILEDDLKAIIkpqYVDQIP--- 177
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIAGLERPTSG---------EVL----------VDGEPVTGPGPDRG---YVFQQDall 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 178 --KAAKGTV--GSILDRKDETKTQAIVCQQLDLTHLKErnVED-----LSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:cd03293 86 pwLTVLDNValGLELQGVPKAEARERAEELLELVGLSG--FENayphqLSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 108773782 249 VKQRLKAAITIRSLINPDRYIIV-VEHDLSVLDYLSDFICCLYGVP 293
Cdd:cd03293 164 ALTREQLQEELLDIWRETGKTVLlVTHDIDEAVFLADRVVVLSARP 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
379-537 |
1.55e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 49.70 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 379 GENGTGKTTFIrMLAGRLKPDEGGEVPV--LNVSYKPQK--------------ISPKSTgsVRQLL-------------- 428
Cdd:COG4604 34 GPNGAGKSTLL-SMISRLLPPDSGEVLVdgLDVATTPSRelakrlailrqenhINSRLT--VRELVafgrfpyskgrlta 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 429 --HEKIRDAythpqfvtdvMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD---SEQrLMaaRV 503
Cdd:COG4604 111 edREIIDEA----------IAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhSVQ-MM--KL 177
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 504 VKRFILHAKKTAFVVEHDFIMATYLADRVIVF-DG 537
Cdd:COG4604 178 LRRLADELGKTVVIVLHDINFASCYADHIVAMkDG 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
373-535 |
1.60e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 48.58 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKStgsvrqllhekIRDAYTHP-QFVTD------V 445
Cdd:cd03215 27 EIVGIAGLVGNGQTELAEALFGLRPPASG------EITLDGKPVTRRS-----------PRDAIRAGiAYVPEdrkregL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 446 MKPLQI-ENIIDQevQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDseqrlMAArvvKRFI------LHAKKTAFVV 518
Cdd:cd03215 90 VLDLSVaENIALS--SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD-----VGA---KAEIyrlireLADAGKAVLL 159
|
170 180
....*....|....*....|
gi 108773782 519 ---EHDFIMAtyLADRVIVF 535
Cdd:cd03215 160 issELDELLG--LCDRILVM 177
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
101-287 |
1.64e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQkPNlGKYDDppdwqEIltYFRGSELQNYFTKILEDDLKAIIKPQ--YVDQIPK 178
Cdd:TIGR02633 25 RPGECVGLCGENGAGKSTLMKILSGVY-PH-GTWDG-----EI--YWSGSPLKASNIRDTERAGIVIIHQEltLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 179 AAKGTVGSILDRKDETKTQAIV---CQQLdLTHLK------ERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:TIGR02633 96 AENIFLGNEITLPGGRMAYNAMylrAKNL-LRELQldadnvTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTE 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 108773782 250 KQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFIC 287
Cdd:TIGR02633 175 KETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTIC 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
102-278 |
2.21e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 49.24 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLG-------KYD--DPPDWQEILTYFR--GSELQNY----FTKILEDDLKA 166
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGqlniaghQFDfsQKPSEKAIRLLRQkvGMVFQQYnlwpHLTVMENLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 167 IIKpqYVDQIPKAAKGTVGSILDRkdetktqaivcqqLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSY 246
Cdd:COG4161 107 PCK--VLGLSKEQAREKAMKLLAR-------------LRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 247 LDVKQRLKAAITIRSLINPDRYIIVVEHDLSV 278
Cdd:COG4161 172 LDPEITAQVVEIIRELSQTGITQVIVTHEVEF 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
96-286 |
2.37e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 96 RLPiprPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYddppdwqeiltyfrgselqnyftKILEddlkaIIKPQYVDQ 175
Cdd:TIGR03719 344 KLP---PGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-----------------------EIGE-----TVKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 176 IPKA--AKGTV-GSILDRKD-------ETKTQAIVC--------QQldlthlkeRNVEDLSGGELQRFACAVVCIQKADI 237
Cdd:TIGR03719 393 SRDAldPNKTVwEEISGGLDiiklgkrEIPSRAYVGrfnfkgsdQQ--------KKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 108773782 238 FMFDEPSSYLDVKqrlkaaiTIRSL----INPDRYIIVVEHDLSVLDYLSDFI 286
Cdd:TIGR03719 465 LLLDEPTNDLDVE-------TLRALeealLNFAGCAVVISHDRWFLDRIATHI 510
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
7-73 |
2.38e-06 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 47.34 E-value: 2.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 7 RIAIVNHD-KCKPKKCRQ----ECKKSCPV--VRMGKLCIEVtpqskiawiSETLCIGCGICIKKCPFGALSIV 73
Cdd:COG1142 37 RIRVVRKAgVSAPVQCRHcedaPCAEVCPVgaITRDDGAVVV---------DEEKCIGCGLCVLACPFGAITMV 101
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
373-534 |
2.47e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.15 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISPKST----------------GSVRQ---------- 426
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAG------EVHYRMRDGQLRDLyalseaerrrllrtewGFVHQhprdglrmqv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 427 ---------LL------HEKIRDAythpqfVTDVMKPLQIE-NIIDQEVQTLSGGELQRVALALCL-GKPADVYLiDEPS 489
Cdd:PRK11701 107 saggnigerLMavgarhYGDIRAT------AGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNLvTHPRLVFM-DEPT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 108773782 490 AYLD-SEQ-RL--MAARVVKRFILhakkTAFVVEHDFIMATYLADRVIV 534
Cdd:PRK11701 180 GGLDvSVQaRLldLLRGLVRELGL----AVVIVTHDLAVARLLAHRLLV 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
337-534 |
2.53e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.35 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 337 ANEEEVKKMcMYKYPGMKKKMGEFELAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLN--VSYKPQ 414
Cdd:PRK13647 2 DNIIEVEDL-HFRYKDGTKALKGLSLSIPEGSKT-----ALLGPNGAGKSTLLLHLNGIYLPQRG-RVKVMGreVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 415 KISPKSTGSVRQLLHEKI------RDAYTHPQ-----------FVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLG 477
Cdd:PRK13647 75 KWVRSKVGLVFQDPDDQVfsstvwDDVAFGPVnmgldkdeverRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 478 KPADVYLIDEPSAYLDSEQRLMAARVVKRfiLHAK-KTAFVVEHDFIMATYLADRVIV 534
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDR--LHNQgKTVIVATHDVDLAAEWADQVIV 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
101-286 |
2.66e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.26 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKqkpnlgkyddpPDWQ----EILtyFRGSELQNyftkiLEDDLKA----IIKPQY 172
Cdd:CHL00131 31 NKGEIHAIMGPNGSGKSTLSKVIAGH-----------PAYKilegDIL--FKGESILD-----LEPEERAhlgiFLAFQY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VDQIP--------KAAKGT--VGSILDRKDETKTQAIVCQQLDLTHLKE----RNV-EDLSGGELQRFACAVVCIQKADI 237
Cdd:CHL00131 93 PIEIPgvsnadflRLAYNSkrKFQGLPELDPLEFLEIINEKLKLVGMDPsflsRNVnEGFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 108773782 238 FMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLS-DFI 286
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYV 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
365-518 |
2.75e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.26 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 365 VAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDeGGEVPVLNVSYKPQKISPKSTGSVRQ--LL--HEKIRDAYTH-- 438
Cdd:PLN03211 87 VTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN-NFTGTILANNRKPTKQILKRTGFVTQddILypHLTVRETLVFcs 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 439 ----PQFVTDVMKPLQIENIIDQE--------------VQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQrlmA 500
Cdd:PLN03211 166 llrlPKSLTKQEKILVAESVISELgltkcentiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA---A 242
|
170
....*....|....*...
gi 108773782 501 ARVVKRFILHAKKTAFVV 518
Cdd:PLN03211 243 YRLVLTLGSLAQKGKTIV 260
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
457-533 |
2.91e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.40 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 457 QEVQTLSGGELQRVALALCLGKPAD---VYLIDEPSAYL--DSEQRLMaaRVVKRFIlHAKKTAFVVEHDF-IMATylAD 530
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfDDIKKLL--EVLQRLV-DKGNTVVVIEHNLdVIKT--AD 899
|
...
gi 108773782 531 RVI 533
Cdd:TIGR00630 900 YII 902
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
101-289 |
2.95e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.35 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLG--------------KYDDPPDWQEILTYFRGSELQNYFTKILEDdlka 166
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdivvsstskQKEIKPVRKKVGVVFQFPESQLFEETVLKD---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 167 iikpqyvdqipkAAKGTVGSILDRKDETKtqaIVCQQLDLTHLK----ERNVEDLSGGELQRFACAVVCIQKADIFMFDE 242
Cdd:PRK13643 106 ------------VAFGPQNFGIPKEKAEK---IAAEKLEMVGLAdefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 108773782 243 PSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDL-SVLDYlSDFICCL 289
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMdDVADY-ADYVYLL 217
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
360-497 |
3.04e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 360 FELAIVageFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKIS----PKSTGSVRQL-------L 428
Cdd:PRK13541 17 FDLSIT---FLPSAITYIKGANGCGKSSLLRMIAGIMQPSSG------NIYYKNCNINniakPYCTYIGHNLglklemtV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108773782 429 HEKIR---DAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQR 497
Cdd:PRK13541 88 FENLKfwsEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
373-518 |
3.06e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.26 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpvlNVSYKPQKISpkstgsvrqllheKIRDAYT-------HPQFVTDV 445
Cdd:PRK13538 28 ELVQIEGPNGAGKTSLLRILAGLARPDAG------EVLWQGEPIR-------------RQRDEYHqdllylgHQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 446 MKPL-------QIENIIDQE------------------VQTLSGGELQRVALA-LCLGKPAdVYLIDEPSAYLDSEQrlm 499
Cdd:PRK13538 89 LTALenlrfyqRLHGPGDDEalwealaqvglagfedvpVRQLSAGQQRRVALArLWLTRAP-LWILDEPFTAIDKQG--- 164
|
170
....*....|....*....
gi 108773782 500 AARVVKRFILHAKKTAFVV 518
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVI 183
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
101-277 |
3.28e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.98 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY---------DDPPDWQEILT-YFR---GSELQNYFTKILEDDLKAI 167
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtARSLSQQKGLIrQLRqhvGFVFQNFNLFPHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 168 IK-PQYVDQIPKAAKGTVGSILDRKdetktqaivcqqLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSY 246
Cdd:PRK11264 107 IEgPVIVKGEPKEEATARARELLAK------------VGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190
....*....|....*....|....*....|.
gi 108773782 247 LDVKQRLKAAITIRSLINPDRYIIVVEHDLS 277
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
101-287 |
3.36e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.42 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY---DDPPDWQEILTYFRGSELQNYFTkiLEDDLKAI----IKPQYV 173
Cdd:PRK13537 31 QRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcGEPVPSRARHARQRVGVVPQFDN--LDPDFTVRenllVFGRYF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 174 DQIPKAAKGTVGSILD-RKDETKTQAivcqqldlthlkerNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQR 252
Cdd:PRK13537 109 GLSAAAARALVPPLLEfAKLENKADA--------------KVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 253 LKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFIC 287
Cdd:PRK13537 175 HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLC 209
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
462-536 |
3.39e-06 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 462 LSGGELQRVALALCLGKPADVYLIDEPSAYLDS--EQRLMAA--RVVKRfilhakKTAFVVEHDF--IMAtylADRVIVF 535
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDThtEREIQAAlrDVSKG------RTTIVIAHRLstIVN---ADKIIVL 208
|
.
gi 108773782 536 D 536
Cdd:cd03253 209 K 209
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
102-275 |
3.50e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGKY-------------DDPPDWQEILTYFrgsELQNYFTKILEDDLkaii 168
Cdd:PRK15064 344 AGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqDHAYDFENDLTLF---DWMSQWRQEGDDEQ---- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 169 kpqyvdqipkAAKGTVGSILDRKDETKTQAIVCqqldlthlkernvedlSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:PRK15064 417 ----------AVRGTLGRLLFSQDDIKKSVKVL----------------SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
170 180 190
....*....|....*....|....*....|.
gi 108773782 249 VKqrlkaaiTIRSLINP-DRY---IIVVEHD 275
Cdd:PRK15064 471 ME-------SIESLNMAlEKYegtLIFVSHD 494
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
7-74 |
3.78e-06 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 48.78 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 7 RIAIVNHDKCKpkKCrQECKKSCPvvrmgKLCIEVTPQSKIAWIS--------------ETLCIGCGICIKKCPFGALSI 72
Cdd:PRK07118 161 GLPVVDEDKCT--GC-GACVKACP-----RNVIELIPKSARVFVAcnskdkgkavkkvcEVGCIGCGKCVKACPAGAITM 232
|
..
gi 108773782 73 VN 74
Cdd:PRK07118 233 EN 234
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
197-287 |
4.08e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.99 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 197 QAIVCQQLDLTHLKERNVEDLSGGE------LQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITI----RSLINPD 266
Cdd:cd03240 96 NVIFCHQGESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIieerKSQKNFQ 175
|
90 100
....*....|....*....|.
gi 108773782 267 ryIIVVEHDLSVLDYLSDFIC 287
Cdd:cd03240 176 --LIVITHDEELVDAADHIYR 194
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
461-587 |
4.08e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.02 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 461 TLSGGELQRVALALCLG-KPADV-YLIDEPSAYL---DSEqRLMAArvvkrfiLHAKK----TAFVVEHD--FIMAtylA 529
Cdd:COG0178 485 TLSGGEAQRIRLATQIGsGLVGVlYVLDEPSIGLhqrDND-RLIET-------LKRLRdlgnTVIVVEHDedTIRA---A 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 530 DRVI-------------VFDGVPSKntVANSPQTLLAgmnKFLS-QLEITF---RRDPNNYRPRI-----NKLNSIkDVE 587
Cdd:COG0178 554 DYIIdigpgagehggevVAQGTPEE--ILKNPDSLTG---QYLSgRKRIPVpkkRRKGNGKFLTIkgareNNLKNV-DVE 627
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
348-536 |
4.11e-06 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 48.38 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 348 YKYPGMKKK-MGEFELAIVAGEftdseiMVML-GENGTGKTTFIRMLAGRLKPDEGG-EVPVLNVSYKPQKISPKSTGSV 424
Cdd:cd03251 8 FRYPGDGPPvLRDISLDIPAGE------TVALvGPSGSGKSTLVNLIPRFYDVDSGRiLIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 425 RQ---LLHEKIRD--AYTHP-----------------QFVTDvmKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADV 482
Cdd:cd03251 82 SQdvfLFNDTVAEniAYGRPgatreeveeaaraanahEFIME--LPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 483 YLIDEPSAYLDSEqrlmAARVVKRFI--LHAKKTAFVVEHDF--IMAtylADRVIVFD 536
Cdd:cd03251 160 LILDEATSALDTE----SERLVQAALerLMKNRTTFVIAHRLstIEN---ADRIVVLE 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
101-277 |
4.25e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.78 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGkqkpnLgkYDdpPDwqeiltyfRGSelqnyftkILED--DLKAIIKPQYVDQIpk 178
Cdd:COG1132 364 PPGETVALVGPSGSGKSTLVNLLLR-----F--YD--PT--------SGR--------ILIDgvDIRDLTLESLRRQI-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 179 aakGTV--------GSILD-----RKDETKTQ-----AIVC---------QQLDlTHLKERNVEdLSGGELQRFACAVVC 231
Cdd:COG1132 417 ---GVVpqdtflfsGTIREnirygRPDATDEEveeaaKAAQahefiealpDGYD-TVVGERGVN-LSGGQRQRIAIARAL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 108773782 232 IQKADIFMFDEPSSYLDVK--QRLKAAitIRSLInPDRYIIVVEHDLS 277
Cdd:COG1132 492 LKDPPILILDEATSALDTEteALIQEA--LERLM-KGRTTIVIAHRLS 536
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
102-291 |
4.66e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 49.06 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLGK---YDDPPDWQEILTYFRGSELQNYFTKILEDDLKA--IIKPQYVdqi 176
Cdd:PRK13536 66 SGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvLGVPVPARARLARARIGVVPQFDNLDLEFTVREnlLVFGRYF--- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 177 pkaakgtvgsildRKDETKTQAIVCQQLDLTHLKER---NVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRL 253
Cdd:PRK13536 143 -------------GMSTREIEAVIPSLLEFARLESKadaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 108773782 254 KAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYG 291
Cdd:PRK13536 210 LIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
8-73 |
4.70e-06 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 44.31 E-value: 4.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 8 IAIVNHDKCKpkKCRqECKKSCPVVrmgklCIEVTPQSKIA-WISETLCIGCGICIKKCPFGALSIV 73
Cdd:COG1146 2 MPVIDTDKCI--GCG-ACVEVCPVD-----VLELDEEGKKAlVINPEECIGCGACELVCPVGAITVE 60
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
101-289 |
4.86e-06 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 47.55 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGkQKPNLGKYddppdwqeiltyfrGSELQNYFtKILEDDLKAIIKpqYVDQipkaa 180
Cdd:cd03213 33 KPGELTAIMGPSGAGKSTLLNALAG-RRTGLGVS--------------GEVLINGR-PLDKRSFRKIIG--YVPQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 kgtvgsildrKDETKTQAIVCQQLDLT-HLKernveDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITI 259
Cdd:cd03213 90 ----------DDILHPTLTVRETLMFAaKLR-----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190
....*....|....*....|....*....|.
gi 108773782 260 RSLINPDRYIIVVEHDLSVLDY-LSDFICCL 289
Cdd:cd03213 155 RRLADTGRTIICSIHQPSSEIFeLFDKLLLL 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
101-247 |
5.11e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEIltYFRGSELQnyftkileddlkaIIKPQ--------Y 172
Cdd:COG3845 29 RPGEIHALLGENGAGKSTLMKILYGLYQPDSG---------EI--LIDGKPVR-------------IRSPRdaialgigM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VDQIPK-------------AAKGTVGSILDRKDETKTQAIVCQQLDLT-HLKERnVEDLSGGELQRfacavVCI-----Q 233
Cdd:COG3845 85 VHQHFMlvpnltvaenivlGLEPTKGGRLDRKAARARIRELSERYGLDvDPDAK-VEDLSVGEQQR-----VEIlkalyR 158
|
170
....*....|....
gi 108773782 234 KADIFMFDEPSSYL 247
Cdd:COG3845 159 GARILILDEPTAVL 172
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
362-537 |
5.56e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTdseimVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSYKPQKISpKSTGSVR------------QLLH 429
Cdd:PRK13649 28 LTIEDGSYT-----AFIGHTGSGKSTIMQLLNGLHVPTQG-SVRVDDTLITSTSKN-KDIKQIRkkvglvfqfpesQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 430 EKI-RDAYTHPQ-FVTDVMKPLQI-----------ENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQ 496
Cdd:PRK13649 101 ETVlKDVAFGPQnFGVSQEEAEALareklalvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 108773782 497 RLMAARVVKRfiLHAK-KTAFVVEHdfIM---ATYlADRVIVFDG 537
Cdd:PRK13649 181 RKELMTLFKK--LHQSgMTIVLVTH--LMddvANY-ADFVYVLEK 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-513 |
5.64e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 49.03 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 355 KKMGEFE-LAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAG--RLKPDEG---------------------GE-VPVLNV 409
Cdd:TIGR03269 8 KKFDGKEvLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiyhvalcekcgyverpskvGEpCPVCGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 410 SYKPQKI-----SPKSTGSVR------------------------QLLHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQ 460
Cdd:TIGR03269 88 TLEPEEVdfwnlSDKLRRRIRkriaimlqrtfalygddtvldnvlEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 108773782 461 TLSGGELQRVALALCLGKPADVYLIDEPSAYLDSeqrlMAARVVKRFILHAKK 513
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP----QTAKLVHNALEEAVK 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
101-286 |
5.71e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 47.75 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK-----YD---DPPDWQEILTYFrGSELqnyftkILEDDLKAIikpQY 172
Cdd:cd03265 24 RRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvagHDvvrEPREVRRRIGIV-FQDL------SVDDELTGW---EN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VdQIPKAAKGTVGSILDRK-DEtktqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQ 251
Cdd:cd03265 94 L-YIHARLYGVPGAERRERiDE------LLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 108773782 252 RLKAAITIRSLI-NPDRYIIVVEHDLSVLDYLSDFI 286
Cdd:cd03265 167 RAHVWEYIEKLKeEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
103-274 |
5.92e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 47.65 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQ--KPNL-------GKYDDPPDWQEILTYFRGSE-LQNYFTkileddlkaiikpqy 172
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRVegGGTTsgqilfnGQPRKPDQFQKCVAYVRQDDiLLPGLT--------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VDQ-IPKAAKGTVGSILDRKDETKTQAIVC-QQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:cd03234 98 VREtLTYTAILRLPRKSSDAIRKKRVEDVLlRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....
gi 108773782 251 QRLKAAITIRSLINPDRYIIVVEH 274
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIH 201
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
2-66 |
6.18e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 46.48 E-value: 6.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 2 ADKLTRI--AIVNHDKC----KPKKCRQeCKKSCPVvrMGKLcIEVTPQSKIAWISETLCIGCGICIKKCP 66
Cdd:cd16373 77 EEQKVKMgvAVIDKDRClawqGGTDCGV-CVEACPT--EAIA-IVLEDDVLRPVVDEDKCVGCGLCEYVCP 143
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
206-285 |
6.43e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 206 LTHLK-ERNVEDLSGGELQRFACAVVCIQKAD--IFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVL--- 279
Cdd:cd03270 126 LGYLTlSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIraa 205
|
....*.
gi 108773782 280 DYLSDF 285
Cdd:cd03270 206 DHVIDI 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
106-304 |
7.13e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.88 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 106 LGLVGTNGIGKSTALKILAGKQKPNLGKY---DDPPDWQEI--LTYFRGSELQN----YFTKILEDDLkaiikpqyvdqi 176
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVlirGEPITKENIreVRKFVGLVFQNpddqIFSPTVEQDI------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 177 pkaAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAA 256
Cdd:PRK13652 101 ---AFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 257 ITIRSLinPDRY---IIVVEHDLSVLDYLSDFICCL-YGVPSAYGVVTMPFS 304
Cdd:PRK13652 178 DFLNDL--PETYgmtVIFSTHQLDLVPEMADYIYVMdKGRIVAYGTVEEIFL 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
379-537 |
9.17e-06 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 47.22 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 379 GENGTGKTTFIRMLAGRLKPDEGgEVPVLNVSYKPQKISP--KSTGSVRQ---LLHEKIRD--AYTHP----QFVTDVMK 447
Cdd:cd03254 36 GPTGAGKTTLINLLMRFYDPQKG-QILIDGIDIRDISRKSlrSMIGVVLQdtfLFSGTIMEniRLGRPnatdEEVIEAAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 448 PLQIENII-------DQEV----QTLSGGELQRVALALCLGKPADVYLIDEPSAYLDS--EQRLMAArvVKRfiLHAKKT 514
Cdd:cd03254 115 EAGAHDFImklpngyDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTetEKLIQEA--LEK--LMKGRT 190
|
170 180
....*....|....*....|....
gi 108773782 515 AFVVEHDfiMATYL-ADRVIVFDG 537
Cdd:cd03254 191 SIIIAHR--LSTIKnADKILVLDD 212
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
2-76 |
9.22e-06 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 47.62 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 2 ADKLTRIAIVNHDKckPKKCRQECKKSCpvvrMG-KLCIEVTPQSKI------AWISETLCIGCGICIKKCPFGALSIVN 74
Cdd:PRK07118 190 KSARVFVACNSKDK--GKAVKKVCEVGC----IGcGKCVKACPAGAItmennlAVIDQEKCTSCGKCVEKCPTKAIRILN 263
|
..
gi 108773782 75 LP 76
Cdd:PRK07118 264 KP 265
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
18-73 |
9.25e-06 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 45.47 E-value: 9.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 18 PKKCRQ--ECKKSCPV--VRMGklciEVTPQSKIAWISETLCIGCGICIKKCPFGALSIV 73
Cdd:cd10549 5 PEKCIGcgICVKACPTdaIELG----PNGAIARGPEIDEDKCVFCGACVEVCPTGAIELT 60
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
369-580 |
9.64e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 369 FTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGG------EVPVLNVSYKPQKISPKSTGSV-----RQLLHEKI-RDAY 436
Cdd:PRK13645 34 FKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyAIPANLKKIKEVKRLRKEIGLVfqfpeYQLFQETIeKDIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 437 THP-----------QFVTDVMKPLQI-ENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVV 504
Cdd:PRK13645 114 FGPvnlgenkqeayKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLF 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 108773782 505 KRFILHAKKTAFVVEHDFIMATYLADRVIVFDgvPSKNTVANSPQTLLAGMnKFLSQLEItfrrDPnnyrPRINKL 580
Cdd:PRK13645 194 ERLNKEYKKRIIMVTHNMDQVLRIADEVIVMH--EGKVISIGSPFEIFSNQ-ELLTKIEI----DP----PKLYQL 258
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
371-537 |
1.01e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 371 DSEIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpVLNVSYKPQKISPKSTGSVRQ---LLHEKIRDAYTHPQF------ 441
Cdd:PRK13639 27 KGEMVALLGPNGAGKSTLFLHFNGILKPTSG----EVLIKGEPIKYDKKSLLEVRKtvgIVFQNPDDQLFAPTVeedvaf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 442 ---------------VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSeqrlMAARVVKR 506
Cdd:PRK13639 103 gplnlglskeevekrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP----MGASQIMK 178
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 507 FILHAKK---TAFVVEHDFIMATYLADRV-IVFDG 537
Cdd:PRK13639 179 LLYDLNKegiTIIISTHDVDLVPVYADKVyVMSDG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
103-262 |
1.06e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 48.02 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKY--------DDPPDWQEILTYFrgselQNY--FTKI-LEDDLKAIIKPQ 171
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqditHVPAENRHVNTVF-----QSYalFPHMtVFENVAFGLRMQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 172 YVdqiPKAakgtvgsildrkdETKTQaiVCQQLDLTHLKE---RNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:PRK09452 115 KT---PAA-------------EITPR--VMEALRMVQLEEfaqRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170
....*....|....
gi 108773782 249 VKQRLKAAITIRSL 262
Cdd:PRK09452 177 YKLRKQMQNELKAL 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
101-243 |
1.10e-05 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 47.15 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeilTYFRGSELQNY-------------------FTKI-L 160
Cdd:cd03218 24 KQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGK-----------ILLDGQDITKLpmhkrarlgigylpqeasiFRKLtV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 161 EDDLKAIIKPQYvdqipkaakgtvgsiLDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQR--FACAVVCiqKADIF 238
Cdd:cd03218 93 EENILAVLEIRG---------------LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRveIARALAT--NPKFL 155
|
....*
gi 108773782 239 MFDEP 243
Cdd:cd03218 156 LLDEP 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
101-248 |
1.14e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 47.37 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeilTYFRGSELqnyfTKILEDDLKAIIKP-QYVDQIPKA 179
Cdd:PRK10419 36 KSGETVALLGRSGCGKSTLARLLVGLESPSQGN-----------VSWRGEPL----AKLNRAQRKAFRRDiQMVFQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 180 A---KGTVGSILD-------RKDETKTQAIVCQQLDLTHLKE----RNVEDLSGGELQRfacavVCIQKA-----DIFMF 240
Cdd:PRK10419 101 AvnpRKTVREIIReplrhllSLDKAERLARASEMLRAVDLDDsvldKRPPQLSGGQLQR-----VCLARAlavepKLLIL 175
|
....*...
gi 108773782 241 DEPSSYLD 248
Cdd:PRK10419 176 DEAVSNLD 183
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
103-248 |
1.14e-05 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 46.72 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKY--------DDPPDWQEILTYFRGSELQNYFTkiLEDDLKAIIKPqyvd 174
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvtAAPPADRPVSMLFQENNLFAHLT--VEQNVGLGLSP---- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 175 qipkaakgtvGSILDRKDETKTQAIVcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:cd03298 98 ----------GLKLTAEDRQAIEVAL-ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
362-507 |
1.29e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 46.76 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 362 LAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGrLKPDEG----GEVPVLNVS---------YKPQKISPKSTGSVRQLL 428
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGeillNGRPLSDWSaaelarhraYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 429 ----HEKIRDAYTHpQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCL------GKPADVYLI-DEPSAYLDSEQR 497
Cdd:COG4138 91 alhqPAGASSEAVE-QLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINPEGQLLLlDEPMNSLDVAQQ 169
|
170
....*....|
gi 108773782 498 LMAARVVKRF 507
Cdd:COG4138 170 AALDRLLREL 179
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
373-537 |
1.32e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.91 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEV-------------------------P---VL-NVSYKP---QK 415
Cdd:COG1126 28 EVVVIIGPSGSGKSTLLRCINLLEEPDSGtitvdGEDltdskkdinklrrkvgmvfqqfnlfPhltVLeNVTLAPikvKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 416 ISPK-STGSVRQLLhEKI-----RDAYthpqfvtdvmkPLQieniidqevqtLSGGELQRVALA--LCLgKPaDVYLIDE 487
Cdd:COG1126 108 MSKAeAEERAMELL-ERVgladkADAY-----------PAQ-----------LSGGQQQRVAIAraLAM-EP-KVMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 488 P-SAyLDSEqrlMAARVVK--RFILHAKKTAFVVEHDfiM--ATYLADRVIVFDG 537
Cdd:COG1126 163 PtSA-LDPE---LVGEVLDvmRDLAKEGMTMVVVTHE--MgfAREVADRVVFMDG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
101-277 |
1.41e-05 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 46.37 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--------YDDPPDWQEILTYFrGSELQNY--FT--KILEDDLKAII 168
Cdd:cd03262 24 KKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTiiidglklTDDKKNINELRQKV-GMVFQQFnlFPhlTVLENITLAPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 169 KpqyVDQIPKA-AKGT-------VGsILDRKDETKTQaivcqqldlthlkernvedLSGGELQRFACAVVCIQKADIFMF 240
Cdd:cd03262 103 K---VKGMSKAeAEERalellekVG-LADKADAYPAQ-------------------LSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 241 DEPSSYLD---VKQRLKaaiTIRSLINPDRYIIVVEHDLS 277
Cdd:cd03262 160 DEPTSALDpelVGEVLD---VMKDLAEEGMTMVVVTHEMG 196
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
4-72 |
1.57e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 44.88 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 4 KLTRIAIV---NHDKCKPKKCRQeCKKscpvvrmgKLCIEVTPQSKIAWISET--------LCIGCGICIKKCPFGALSI 72
Cdd:cd10550 29 SLSRIRVVrfePEGLDVPVVCRQ-CED--------APCVEACPVGAISRDEETgavvvdedKCIGCGMCVEACPFGAIRV 99
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
373-493 |
1.65e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 46.56 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEV----PV-----LNVSYKPQkispksTGSV-RQL---------- 427
Cdd:COG1137 30 EIVGLLGPNGAGKTTTFYMIVGLVKPDSGrifldGEDithlPMhkrarLGIGYLPQ------EASIfRKLtvednilavl 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 428 -LHEKIRDAYThpQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCL-GKPaDVYLIDEPSAYLD 493
Cdd:COG1137 104 eLRKLSKKERE--ERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALaTNP-KFILLDEPFAGVD 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
361-530 |
1.94e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 361 ELAIVAGEftdseiMVML-GENGTGKTTFIRMLAGRLKPDEGgEVPV---LNVSyKPQKISPKS-TGSV----------- 424
Cdd:PRK11147 23 ELHIEDNE------RVCLvGRNGAGKSTLMKILNGEVLLDDG-RIIYeqdLIVA-RLQQDPPRNvEGTVydfvaegieeq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 425 -------RQLLH-------EKIRDAYTHPQFVTDVMKPLQIENII-----------DQEVQTLSGGELQRVALALCLGKP 479
Cdd:PRK11147 95 aeylkryHDISHlvetdpsEKNLNELAKLQEQLDHHNLWQLENRInevlaqlgldpDAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 480 ADVYLIDEPSAYLDSEqrlmAARVVKRFILHAKKTAFVVEHD--FI--MATYLAD 530
Cdd:PRK11147 175 PDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDrsFIrnMATRIVD 225
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
457-533 |
2.02e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.45 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 457 QEVQTLSGGELQRVALALCLGKPAD---VYLIDEPSAYL--DSEQRLMaarVVKRFILHAKKTAFVVEHDF-IMATylAD 530
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfHDVKKLL---EVLQRLVDKGNTVVVIEHNLdVIKC--AD 239
|
...
gi 108773782 531 RVI 533
Cdd:cd03271 240 WII 242
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
17-69 |
2.03e-05 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 44.69 E-value: 2.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 17 KPKKCRQ----ECKKSCPVvrmgkLCIEVTPqSKIAWISETLCIGCGICIKKCPFGA 69
Cdd:cd04410 46 LPVSCMHcedpPCVKACPT-----GAIYKDE-DGIVLIDEDKCIGCGSCVEACPYGA 96
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
350-529 |
2.05e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 46.23 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 350 YPGmKKKMGEFELAIVAGEftdseIMVMLGENGTGKTTFIRMLAGRLKPDEGgevpVLNVSYKPQKISPKSTGSVRQllH 429
Cdd:PRK11248 11 YGG-KPALEDINLTLESGE-----LLVVLGPSGCGKTTLLNLIAGFVPYQHG----SITLDGKPVEGPGAERGVVFQ--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 430 EKI---RDAYTHPQF---------------VTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAY 491
Cdd:PRK11248 79 EGLlpwRNVQDNVAFglqlagvekmqrleiAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 108773782 492 LDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLA 529
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
376-537 |
2.13e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 376 VMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQK--ISpksTGSVR-QLLH------EKIRDAYTHPQFVTDVM 446
Cdd:PTZ00243 690 VVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQawIM---NATVRgNILFfdeedaARLADAVRVSQLEADLA 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 447 K-PLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEqrlMAARVVKRFILH--AKKTAFVVEH--- 520
Cdd:PTZ00243 767 QlGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH---VGERVVEECFLGalAGKTRVLATHqvh 843
|
170 180
....*....|....*....|..
gi 108773782 521 -----DFIMAtyLADRVIVFDG 537
Cdd:PTZ00243 844 vvpraDYVVA--LGDGRVEFSG 863
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
205-291 |
2.32e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.18 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 205 DLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSL-INPDRYIIVVEHDLSVLDYLS 283
Cdd:PRK14258 139 EIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQVSRLS 218
|
....*...
gi 108773782 284 DFICCLYG 291
Cdd:PRK14258 219 DFTAFFKG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
377-506 |
2.42e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.31 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 377 MLGENGTGKTTFIRMLAGRlkpDEGGEVP-VLNVSYKPQKIS-PKSTGSVRQLlhekirdaYTHPQFVTdVMKPLQIENI 454
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGR---KTAGVITgEILINGRPLDKNfQRSTGYVEQQ--------DVHSPNLT-VREALRFSAL 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 108773782 455 IdqevQTLSGGELQRVALALCL-GKPADVYLiDEPSAYLDSEQRLMAARVVKR 506
Cdd:cd03232 106 L----RGLSVEQRKRLTIGVELaAKPSILFL-DEPTSGLDSQAAYNIVRFLKK 153
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
101-290 |
2.45e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQkpnlgkyDDPPDWQEILtyFRGSELQNyftkiLEDDLKA----IIKPQYVDQI 176
Cdd:PRK09580 25 RPGEVHAIMGPNGSGKSTLSATLAGRE-------DYEVTGGTVE--FKGKDLLE-----LSPEDRAgegiFMAFQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 177 PKAA-----KGTVGSI--------LDRKD-----ETKTQAIVCQQLDLThlkeRNV-EDLSGGELQRFACAVVCIQKADI 237
Cdd:PRK09580 91 PGVSnqfflQTALNAVrsyrgqepLDRFDfqdlmEEKIALLKMPEDLLT----RSVnVGFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 108773782 238 FMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLS-DFICCLY 290
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLY 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
102-257 |
2.76e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.64 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKPNLG--KYDDppdwqeiltyfRGSELQNYFTKIleddlkaiikpQYV---Dqi 176
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtiKLDG-----------GDIDDPDVAEAC-----------HYLghrN-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 177 pkAAKG--TVG-------SILDRKDETKTQAIVCQQL-DLTHLKERNvedLSGGELQRFACAVVCIQKADIFMFDEPSSY 246
Cdd:PRK13539 83 --AMKPalTVAenlefwaAFLGGEELDIAAALEAVGLaPLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|..
gi 108773782 247 LDVK-QRLKAAI 257
Cdd:PRK13539 158 LDAAaVALFAEL 169
|
|
| IOR_alpha |
TIGR03336 |
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin ... |
10-70 |
2.78e-05 |
|
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.
Pssm-ID: 274526 [Multi-domain] Cd Length: 595 Bit Score: 47.03 E-value: 2.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 108773782 10 IVNHDKCKpkKCRQeCKKS--CPVVRMGKLCIEVTPqskiawisetLCIGCGICIKKCPFGAL 70
Cdd:TIGR03336 546 KVDQDKCI--GCKK-CIKElgCPAIEPEDKEAVIDP----------LCTGCGVCAQICPFDAI 595
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
7-86 |
3.05e-05 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 47.05 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 7 RIAIVNHDKCK-PKKCRQ----ECKKSCP---VVRMGKlCIEVTPQSkiawisetlCIGCGICIKKCPFGALSIVNLP-- 76
Cdd:PRK12769 41 RITVIKHQQQRsAVTCHHcedaPCARSCPngaISHVDD-SIQVNQQK---------CIGCKSCVVACPFGTMQIVLTPva 110
|
90
....*....|
gi 108773782 77 SNLEKETTHR 86
Cdd:PRK12769 111 AGKVKATAHK 120
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
456-547 |
3.18e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 456 DQEVQTLSGGELQRVALALCLGKP--ADVYLIDEPSAYLDSEQRLMAARVVKRfILHAKKTAFVVEHDFIMATyLADRVI 533
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQDTHKLINVIKK-LRDQGNTVLLVEHDEQMIS-LADRII 548
|
90 100
....*....|....*....|....*..
gi 108773782 534 -------------VFDGVPsKNTVANS 547
Cdd:PRK00635 549 digpgagifggevLFNGSP-REFLAKS 574
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
461-533 |
3.24e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 461 TLSGGELQRVALALCLGKPAD---VYLIDEPSAYLDSE--QRLMAArvvkrfiLH----AKKTAFVVEH--DFIMAtylA 529
Cdd:COG0178 826 TLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHdiRKLLEV-------LHrlvdKGNTVVVIEHnlDVIKT---A 895
|
....
gi 108773782 530 DRVI 533
Cdd:COG0178 896 DWII 899
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
103-290 |
3.50e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.73 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLG-------------------KYDDPPDWQEILT----YFRGSELQNYFTkI 159
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqtinlvrdkdgqlKVADKNQLRLLRTrltmVFQHFNLWSHMT-V 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 160 LEDDLKAiikPQYVDQIPKAakgtvgsildrkdETKTQAIvcQQLDLTHLKERNVE----DLSGGELQRFACAVVCIQKA 235
Cdd:PRK10619 110 LENVMEA---PIQVLGLSKQ-------------EARERAV--KYLAKVGIDERAQGkypvHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 236 DIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLY 290
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
365-536 |
4.64e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.85 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 365 VAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEG------------------GEVPVLNVSYKPQKISPKSTGSVR- 425
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekEKVLEKLVIQKTRFKKIKKIKEIRr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 426 -----------QLLHEKI-RDAYTHP-QFVTDVMKPLQI-----------ENIIDQEVQTLSGGELQRVALALCLGKPAD 481
Cdd:PRK13651 106 rvgvvfqfaeyQLFEQTIeKDIIFGPvSMGVSKEEAKKRaakyielvgldESYLQRSPFELSGGQKRRVALAGILAMEPD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 108773782 482 VYLIDEPSAYLDSEQRLMAARVVKRfiLHAK-KTAFVVEHDFIMATYLADRVIVFD 536
Cdd:PRK13651 186 FLVFDEPTAGLDPQGVKEILEIFDN--LNKQgKTIILVTHDLDNVLEWTKRTIFFK 239
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
50-74 |
5.12e-05 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 41.64 E-value: 5.12e-05
10 20
....*....|....*....|....*
gi 108773782 50 ISETLCIGCGICIKKCPFGALSIVN 74
Cdd:COG2768 8 VDEEKCIGCGACVKVCPVGAISIED 32
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
213-281 |
5.21e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 5.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 213 NVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLI-NPDRYIIVVEHDLSVLDY 281
Cdd:PTZ00265 576 NASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRY 645
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
101-277 |
5.30e-05 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 44.84 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILagkqkpnLGKYDdpPDWQEILtyFRGSELQNYFTKiledDLKAIIKpqYVDQIPKAA 180
Cdd:cd03249 27 PPGKTVALVGSSGCGKSTVVSLL-------ERFYD--PTSGEIL--LDGVDIRDLNLR----WLRSQIG--LVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTVGS--ILDRKDETKTQAI-VCQQLDL------------THLKERNVEdLSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:cd03249 90 DGTIAEniRYGKPDATDEEVEeAAKKANIhdfimslpdgydTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 108773782 246 YLD------VKQRLKAAITirslinpDRYIIVVEHDLS 277
Cdd:cd03249 169 ALDaeseklVQEALDRAMK-------GRTTIVIAHRLS 199
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
379-493 |
5.35e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.56 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 379 GENGTGKTTFIRMLAGRLKPdEGGEVPVLNVS-------YKPQ--------KISPKSTgsVRQLLHEKIRDAYTHPQfVT 443
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNP-EKGEILFERQSikkdlctYQKQlcfvghrsGINPYLT--LRENCLYDIHFSPGAVG-IT 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 108773782 444 DVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD 493
Cdd:PRK13540 110 ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
101-262 |
5.48e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGkqkpNLGKYDDPpdwqeiltyfRGSELQNYFTkILEDDLKAIIKPQY-------- 172
Cdd:PRK13547 25 EPGRVTALLGRNGAGKSTLLKALAG----DLTGGGAP----------RGARVTGDVT-LNGEPLAAIDAPRLarlravlp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 ----------VDQI------PKAAKGTVGSILDRkdETKTQAIvcQQLDLTHLKERNVEDLSGGELQRFACAVVCIQ--- 233
Cdd:PRK13547 90 qaaqpafafsAREIvllgryPHARRAGALTHRDG--EIAWQAL--ALAGATALVGRDVTTLSGGELARVQFARVLAQlwp 165
|
170 180 190
....*....|....*....|....*....|....*
gi 108773782 234 ------KADIFMFDEPSSYLDVKQRLKAAITIRSL 262
Cdd:PRK13547 166 phdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRL 200
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
103-281 |
6.07e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.00 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGkqkpnLGKYDDPPDWQ-EILtyfrGSELQNYfTKILEDDLKAIIKPQYVDQ------ 175
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLSG-----LITGDKSAGSHiELL----GRTVQRE-GRLARDIRKSRANTGYIFQqfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 176 ----IPKAAKGTVGS----------ILDRKDETKTQAIVcqQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFD 241
Cdd:PRK09984 100 rlsvLENVLIGALGStpfwrtcfswFTREQKQRALQALT--RVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 242 EPSSYLDVKQRLKAAITIRSLINPDRYIIVVEhdLSVLDY 281
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVT--LHQVDY 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
101-248 |
6.24e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 44.75 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKP----------NLGKYddPPD-------WQEiltyfrgselQNYFTKI---- 159
Cdd:COG3840 23 AAGERVAILGPSGAGKSTLLNLIAGFLPPdsgrilwngqDLTAL--PPAerpvsmlFQE----------NNLFPHLtvaq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 160 -----LEDDLKaiikpqyvdqipkaakgtvgsiLDRKDETKTQAIvCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQK 234
Cdd:COG3840 91 niglgLRPGLK----------------------LTAEQRAQVEQA-LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170
....*....|....
gi 108773782 235 ADIFMFDEPSSYLD 248
Cdd:COG3840 148 RPILLLDEPFSALD 161
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
2-74 |
6.47e-05 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 45.79 E-value: 6.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 2 ADKLTRIAIVNH-DKCKPKKCRQ----ECKKSCPVVRMgklcievTPQSKIAWISETLCIGCGICIKKCPFGALSIVN 74
Cdd:PRK12809 36 SDFRPRIHVVGKgQAANPVACHHcnnaPCVTACPVNAL-------TFQSDSVQLDEQKCIGCKRCAIACPFGVVEMVD 106
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
48-71 |
7.22e-05 |
|
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 39.92 E-value: 7.22e-05
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
3-73 |
7.47e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 42.56 E-value: 7.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 3 DKLTRIAIVNHDKCKpkKCRQeCKKSCPVVRMGklcieVTPQSKIAWISeTLCIGCGICIKKCPFGALSIV 73
Cdd:cd10550 69 DEETGAVVVDEDKCI--GCGM-CVEACPFGAIR-----VDPETGKAIKC-DLCGGDPACVKVCPTGALEFV 130
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
449-548 |
8.37e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.49 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 449 LQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSE--QRLMAarvvkrfILHAKK----TAFVVEHDF 522
Cdd:PRK10535 132 LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHsgEEVMA-------ILHQLRdrghTVIIVTHDP 204
|
90 100
....*....|....*....|....*..
gi 108773782 523 IMATYlADRVI-VFDGvpskNTVANSP 548
Cdd:PRK10535 205 QVAAQ-AERVIeIRDG----EIVRNPP 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
70-276 |
8.92e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 44.70 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 70 LSIVNLPSNLEKET-THRYCANAFKLHRlpiprpGEVLGLVGTNGIGKSTALKILAG--KQKPNLGKYDDPPDWQEILTY 146
Cdd:PRK13642 5 LEVENLVFKYEKESdVNQLNGVSFSITK------GEWVSIIGQNGSGKSTTARLIDGlfEEFEGKVKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 147 FR---GSELQN----YFTKILEDDLKAIIKPQyvdQIPKAakgtvgSILDRKDETktqAIVCQQLDLthlKERNVEDLSG 219
Cdd:PRK13642 79 LRrkiGMVFQNpdnqFVGATVEDDVAFGMENQ---GIPRE------EMIKRVDEA---LLAVNMLDF---KTREPARLSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 220 GELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLinPDRY---IIVVEHDL 276
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI--KEKYqltVLSITHDL 201
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
27-73 |
1.16e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.85 E-value: 1.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 108773782 27 KSCPVVRMGKLCIEVTpqskIAWISETLCIGCGICIKKCPFGALSIV 73
Cdd:COG1148 474 RAIQLLSKGELGVEPS----VAEVDPEKCTGCGRCVEVCPYGAISID 516
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
361-517 |
1.17e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 361 ELAIVAGEFtdseiMVMLGENGTGKTTFIRMLAGRLKPDEGGEV-----PVLNVSYKPQKI-------------SPKS-- 420
Cdd:PRK10938 23 SLTLNAGDS-----WAFVGANGSGKSALARALAGELPLLSGERQsqfshITRLSFEQLQKLvsdewqrnntdmlSPGEdd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 421 TG-SVRQLLHEKIRDaythPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLM 499
Cdd:PRK10938 98 TGrTTAEIIQDEVKD----PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|....*...
gi 108773782 500 AARVVKRfiLHAKKTAFV 517
Cdd:PRK10938 174 LAELLAS--LHQSGITLV 189
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
101-289 |
1.28e-04 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 43.58 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK--YDD------PPDwqEILTyfRG----SELQNYFTKI-LEDDLKai 167
Cdd:cd03224 24 PEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirFDGrditglPPH--ERAR--AGigyvPEGRRIFPELtVEENLL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 168 ikpqyvdqipkaakgtVGSILDRKDETKtqAIVCQQLDL-THLKER---NVEDLSGGELQRFACAVVCIQKADIFMFDEP 243
Cdd:cd03224 98 ----------------LGAYARRRAKRK--ARLERVYELfPRLKERrkqLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 108773782 244 SSYLD---VKQRLKAAITIRSLinpDRYIIVVEHDLSVLDYLSDFICCL 289
Cdd:cd03224 160 SEGLApkiVEEIFEAIRELRDE---GVTILLVEQNARFALEIADRAYVL 205
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
12-74 |
1.29e-04 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 43.83 E-value: 1.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 12 NHDKCKPKkCRQECKKSCPVVRMG--KLCievtpqskiawisETLCIGCGICIKKCPFGALSIVN 74
Cdd:COG2878 108 GCEKAKPK-YEYDGIKDCRAAVIGgpKGC-------------EYGCIGCGDCIKACPFDAIVGAA 158
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
8-74 |
1.51e-04 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 43.56 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 108773782 8 IAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVN 74
Cdd:COG1145 137 AALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKD 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
460-542 |
1.58e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 460 QTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDfIMATYLADRVIVFDGvP 539
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR-IASIKRSDKIVVFNN-P 1434
|
...
gi 108773782 540 SKN 542
Cdd:PTZ00265 1435 DRT 1437
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
368-497 |
1.72e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 368 EFtDSEIMVMLGENGTGKTTFIRMLAGRLKpdegGEVPvlnvsykPQKispKSTGSVRQLLHEKIRDAYTHPQFVTDVMK 447
Cdd:cd03240 19 EF-FSPLTLIVGQNGAGKTTIIEALKYALT----GELP-------PNS---KGGAHDPKLIREGEVRAQVKLAFENANGK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 448 PLQIEN------------------IIDQEVQTLSGGE------LQRVALALCLGKPADVYLIDEPSAYLDSEQR 497
Cdd:cd03240 84 KYTITRslailenvifchqgesnwPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENI 157
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
8-72 |
1.91e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.47 E-value: 1.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108773782 8 IAIVNHDKCKpkkcrqeckkSCpvvrmgKLCIEVTPQSKI-------AWISETLCIGCGICIKKCPFGALSI 72
Cdd:COG1148 490 VAEVDPEKCT----------GC------GRCVEVCPYGAIsidekgvAEVNPALCKGCGTCAAACPSGAISL 545
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
101-277 |
1.91e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.16 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALK------------ILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFTKiLEDdlkaii 168
Cdd:PRK09493 25 DQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTA-LEN------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 169 kpqyVDQIPKAAKGTvgsildRKDETKTQAIvcQQLDLTHLKERN---VEDLSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:PRK09493 98 ----VMFGPLRVRGA------SKEEAEKQAR--ELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 246 YLDVKQRLKAAITIRSLINPDRYIIVVEHDLS 277
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
102-125 |
1.99e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.92 E-value: 1.99e-04
10 20
....*....|....*....|....
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAG 125
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTG 70
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
101-289 |
2.10e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQkPNlGKYDDppdwqEIltYFRGSELQNYFTKILEDDLKAIIKPQ--YVDQIPK 178
Cdd:PRK13549 29 RAGEIVSLCGENGAGKSTLMKVLSGVY-PH-GTYEG-----EI--IFEGEELQASNIRDTERAGIAIIHQElaLVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 179 AAKGTVGSILDRKDETKTQAIV--CQQLdLTHLK-----ERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQ 251
Cdd:PRK13549 100 LENIFLGNEITPGGIMDYDAMYlrAQKL-LAQLKldinpATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESE 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 108773782 252 -RLKAAItIRSLINPDRYIIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK13549 179 tAVLLDI-IRDLKAHGIACIYISHKLNEVKAISDTICVI 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
361-488 |
2.38e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 361 ELAIVA-------GEFT--D--------SEIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEvPV--------LNVS 410
Cdd:NF033858 264 EPAIEArgltmrfGDFTavDhvsfrirrGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfGQ-PVdagdiatrRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 411 YKPQKISPKSTGSVRQ--LLH--------EKIrdaythPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALAL-CLGKP 479
Cdd:NF033858 343 YMSQAFSLYGELTVRQnlELHarlfhlpaAEI------AARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVaVIHKP 416
|
....*....
gi 108773782 480 aDVYLIDEP 488
Cdd:NF033858 417 -ELLILDEP 424
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
374-537 |
2.51e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 43.33 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 374 IMVMLGENGTGKTTFIRMLAGRLKPDEGgEVPVLN-----------VSYKPQkiSPKSTGSVRQLLHEKI---------- 432
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALMGFVRLASG-KISILGqptrqalqknlVAYVPQ--SEEVDWSFPVLVEDVVmmgryghmgw 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 433 -RDAYTHP-QFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLD--SEQRLMAarvVKRFI 508
Cdd:PRK15056 112 lRRAKKRDrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDvkTEARIIS---LLREL 188
|
170 180
....*....|....*....|....*....
gi 108773782 509 LHAKKTAFVVEHDFIMATYLADRVIVFDG 537
Cdd:PRK15056 189 RDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| FDH_beta_like |
cd16366 |
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
25-69 |
2.55e-04 |
|
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.
Pssm-ID: 319888 [Multi-domain] Cd Length: 156 Bit Score: 41.62 E-value: 2.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 108773782 25 CKKSCPVVRMGKlcievTPQSKIAWISETlCIGCGICIKKCPFGA 69
Cdd:cd16366 78 CLAACPTGAIIR-----TETGTVVVDPET-CIGCGYCVNACPFDI 116
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
462-536 |
2.60e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.80 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 462 LSGGELQRVALALCLGKPADVYLIDEPSAYLDS--EQRLMAA--RVVKrfilhaKKTAFVVEHDfiMATYL-ADRVIVFD 536
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVetEAKVKAAldELMK------GRTTFIIAHR--LSTVRnADRILVFD 543
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
55-74 |
3.11e-04 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 40.84 E-value: 3.11e-04
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
103-294 |
4.08e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 42.73 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKY----DDPPDWQEILTYFR---GSELQNYFTKILEDDLKAIIkpqyvdq 175
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgVDITDKKVKLSDIRkkvGLVFQYPEYQLFEETIEKDI------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 176 ipkaAKGTVGSILDrKDETKT---QAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQR 252
Cdd:PRK13637 106 ----AFGPINLGLS-EEEIENrvkRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 253 LKAAITIRSLinPDRY---IIVVEHDLSVLDYLSDFI-------CCLYGVPS 294
Cdd:PRK13637 181 DEILNKIKEL--HKEYnmtIILVSHSMEDVAKLADRIivmnkgkCELQGTPR 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
99-286 |
4.17e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 41.93 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 99 IPRpGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDdppdWQEILTYFRGSElqnyftkilEDDLKAIIKPQYVDQIPK 178
Cdd:cd03290 24 IPT-GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH----WSNKNESEPSFE---------ATRSRNRYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 179 AAKGTV------GSILDRKD-ETKTQAIVCQ-QLDL------THLKERNVeDLSGGELQRFACAVVCIQKADIFMFDEPS 244
Cdd:cd03290 90 LLNATVeenitfGSPFNKQRyKAVTDACSLQpDIDLlpfgdqTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 108773782 245 SYLDV--KQRLKAAITIRSLINPDRYIIVVEHDLSVLDYlSDFI 286
Cdd:cd03290 169 SALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWI 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
461-533 |
4.35e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 461 TLSGGELQRVALALCLGK--PADVYLIDEPSAYL---DSEqRLMAArvvkrfILHAKK---TAFVVEHDFIMATyLADRV 532
Cdd:TIGR00630 488 TLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLhqrDNR-RLINT------LKRLRDlgnTLIVVEHDEDTIR-AADYV 559
|
.
gi 108773782 533 I 533
Cdd:TIGR00630 560 I 560
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
462-537 |
4.55e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 43.28 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 462 LSGGELQRVALALCLGKPADVYLIDEPSAYLDS--EQRLMAArvvkrFILHAK-KTAFVVEHDfimATYLA--DRVIVFD 536
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAetERQILEL-----LAEHAQnKTVLMITHR---LTGLEqfDRICVMD 547
|
.
gi 108773782 537 G 537
Cdd:PRK11160 548 N 548
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
101-284 |
4.79e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.51 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDdppdwqeILTYFRGSELQNyftkileDDLKAIIKP-QYVDQIPKA 179
Cdd:PRK13641 31 EEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTIT-------IAGYHITPETGN-------KNLKKLRKKvSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 180 A--KGTVGSILD--------RKDETKTQAIvcQQLDLTHLKERNVE----DLSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:PRK13641 97 QlfENTVLKDVEfgpknfgfSEDEAKEKAL--KWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 246 YLDVKQRLKAAITIRSLINPDRYIIVVEHDL-SVLDYLSD 284
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADD 214
|
|
| DMSOR_beta_like |
cd16371 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
38-69 |
4.93e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319893 [Multi-domain] Cd Length: 140 Bit Score: 40.62 E-value: 4.93e-04
10 20 30
....*....|....*....|....*....|....*....
gi 108773782 38 CIEVTPQ---SK----IAWISETLCIGCGICIKKCPFGA 69
Cdd:cd16371 62 CVKVCPTgaiTKredgIVVVDQDKCIGCGYCVWACPYGA 100
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
374-537 |
4.96e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 43.40 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 374 IMVMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQKISPKSTgSVR-------QLLHEKIRDAYTHPQFVTDV- 445
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQND-SLRenilfgkALNEKYYQQVLEACALLPDLe 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 446 MKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSE-QRLMAARVVKRFILHAKKTAFVVEHDFim 524
Cdd:TIGR00957 745 ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEGVLKNKTRILVTHGI-- 822
|
170
....*....|....*
gi 108773782 525 aTYL--ADRVIVFDG 537
Cdd:TIGR00957 823 -SYLpqVDVIIVMSG 836
|
|
| DMSOR_beta_like |
cd16374 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
18-81 |
5.13e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319896 [Multi-domain] Cd Length: 139 Bit Score: 40.72 E-value: 5.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 18 PKKCRQeCKKSCpvvrmgklCIEVTPQSKI-------AWISETLCIGCGICIKKCPFGALSIVNLPSNLEK 81
Cdd:cd16374 40 PVRCRH-CEDAP--------CMEVCPTGAIyrdedgaVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVK 101
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
457-518 |
5.26e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 41.86 E-value: 5.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 108773782 457 QEVQTLSGGELQRVALAL--CLGK--PADVYLIDEPSAYLDSEQRLMAARVVKRFilhAKKTAFVV 518
Cdd:cd03272 154 QEMQQLSGGQKSLVALALifAIQKcdPAPFYLFDEIDAALDAQYRTAVANMIKEL---SDGAQFIT 216
|
|
| PorD_KorD |
TIGR02179 |
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number ... |
10-73 |
6.21e-04 |
|
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of delta subunits, representing mostly pyruvate, 2-ketoisovalerate, and 2-oxoglutarate specific enzymes. The delta subunit is the smallest and resembles ferredoxins.
Pssm-ID: 131234 [Multi-domain] Cd Length: 78 Bit Score: 38.85 E-value: 6.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 10 IVNHDKCKpkKCRqECKKSCPvvrmgKLCIEVTPQSKIAwISETLCIGCGICIKKCPFGALSIV 73
Cdd:TIGR02179 21 VVDKEKCI--KCK-NCWLYCP-----EGAIQEDEGGFVG-IDYDYCKGCGICANVCPVKAIEMV 75
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
3-74 |
6.77e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 42.32 E-value: 6.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108773782 3 DKLTRIAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIawISETLCIGCGICIKKCPFGALSIVN 74
Cdd:COG4624 43 DDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSII--RDKEKCKNCYPCVRACPVKAIKVDD 112
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
43-69 |
6.97e-04 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 41.08 E-value: 6.97e-04
10 20
....*....|....*....|....*..
gi 108773782 43 PQSKIAWISETLCIGCGICIKKCPFGA 69
Cdd:PRK05113 104 PARKVAFIDEDNCIGCTKCIQACPVDA 130
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
1-72 |
7.08e-04 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 41.59 E-value: 7.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 1 MADKLTRIAIVNHDKCKpkKCRQeCKKSCPV---VRMGKLcievtPQSKiawisetlCIGCGICIKKCPFGALSI 72
Cdd:COG0348 197 LSDLSTLRVRYDRGDCI--DCGL-CVKVCPMgidIRKGEI-----NQSE--------CINCGRCIDACPKDAIRF 255
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
373-534 |
7.98e-04 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 41.96 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPD--EGGEVpvlnvSYKPQKISPKSTGSVRQLLHEKI----RDAYT--HPqfvtd 444
Cdd:COG0444 32 ETLGLVGESGSGKSTLARAILGLLPPPgiTSGEI-----LFDGEDLLKLSEKELRKIRGREIqmifQDPMTslNP----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 445 VMK-------PLQIENIID------------QEVQ-------------TLSGGELQRV--ALALCLgKPaDVyLI-DEPS 489
Cdd:COG0444 102 VMTvgdqiaePLRIHGGLSkaeareraiellERVGlpdperrldryphELSGGMRQRVmiARALAL-EP-KL-LIaDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 108773782 490 AYLD-SEQR----LMaARVVKRFilhakKTAFV-VEHDFIMATYLADRVIV 534
Cdd:COG0444 179 TALDvTIQAqilnLL-KDLQREL-----GLAILfITHDLGVVAEIADRVAV 223
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
47-74 |
8.48e-04 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 38.15 E-value: 8.48e-04
10 20
....*....|....*....|....*...
gi 108773782 47 IAWISETLCIGCGICIKKCPFGALSIVN 74
Cdd:COG1146 2 MPVIDTDKCIGCGACVEVCPVDVLELDE 29
|
|
| PhsB_like |
cd10553 |
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ... |
24-69 |
8.55e-04 |
|
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319875 [Multi-domain] Cd Length: 146 Bit Score: 40.04 E-value: 8.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 108773782 24 ECKKSCPVVRMGKlcievTPQSKIAWISETLCIGCGICIKKCPFGA 69
Cdd:cd10553 65 WCVKACPTGAMQK-----REKDGIVYVDQELCIGCKACIEACPWGI 105
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
461-530 |
9.06e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 461 TLSGGELQRVALALCLGKPAD---VYLIDEPSAYLDSE--QRLMAarvvkrfILH----AKKTAFVVEH--DFI-MATYL 528
Cdd:PRK00349 830 TLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEdiRKLLE-------VLHrlvdKGNTVVVIEHnlDVIkTADWI 902
|
..
gi 108773782 529 AD 530
Cdd:PRK00349 903 ID 904
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
102-214 |
9.53e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTALKILAGKQKP--------NLGKYDDPPDWQEILTYFRGSELQNYFTKILEDDLKAIIKPQY- 172
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPpgggviyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPd 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 108773782 173 ---VDqipkaakgTVGSILDRKDETKTQAIVCQQLDLTHLKERNV 214
Cdd:smart00382 81 vliLD--------EITSLLDAEQEALLLLLEELRLLLLLKSEKNL 117
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
373-508 |
9.70e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.31 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 373 EIMVMLGENGTGKTTFIRMLAGRLKPDEG-----GEVPVLNVS-------YKPQ--KISPKSTGSVRQLLHEKIRDAYTH 438
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvaGKSILTNISdvhqnmgYCPQfdAIDDLLTGREHLYLYARLRGVPAE 2045
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 108773782 439 P-QFVTD-VMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFI 508
Cdd:TIGR01257 2046 EiEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
205-248 |
1.21e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.89 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 108773782 205 DLTHLKERNVeDLSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:PLN03232 730 DLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
18-66 |
1.21e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 37.23 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 18 PKKCRQ--ECKKSCPVVRMGKLCIEVTPQ-SKIAWISETlCIGCGICIKKCP 66
Cdd:pfam13237 6 PDKCIGcgRCTAACPAGLTRVGAIVERLEgEAVRIGVWK-CIGCGACVEACP 56
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
40-70 |
1.22e-03 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 39.78 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|.
gi 108773782 40 EVTPQSKIAWISETLCIGCGICIKKCPFGAL 70
Cdd:TIGR01944 100 GTIQPPMVALIDEDNCIGCTKCIQACPVDAI 130
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
204-262 |
1.24e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.37 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 204 LDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSL 262
Cdd:PRK11650 122 LELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRL 180
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
103-281 |
1.31e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.23 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILTYFRGSELQNYFTKILEDDLKAIIKPQYVDQIP--KAA 180
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFIEHLNALLLPDTG---------TIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKkiKEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTVGSILD------------------------RKDETKTQA---IVCQQLDLTHLkERNVEDLSGGELQRFACAVVCIQ 233
Cdd:PRK13651 104 RRRVGVVFQfaeyqlfeqtiekdiifgpvsmgvSKEEAKKRAakyIELVGLDESYL-QRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 234 KADIFMFDEPSSYLD---VKQRLKaaiTIRSLINPDRYIIVVEHDL-SVLDY 281
Cdd:PRK13651 183 EPDFLVFDEPTAGLDpqgVKEILE---IFDNLNKQGKTIILVTHDLdNVLEW 231
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
55-76 |
1.40e-03 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 36.76 E-value: 1.40e-03
|
| FDH-O_like |
cd10560 |
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
14-68 |
1.54e-03 |
|
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.
Pssm-ID: 319882 [Multi-domain] Cd Length: 225 Bit Score: 40.45 E-value: 1.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 14 DKCKpkKCRQE-CKKSCPV---VRmgklcievTPQSKIaWISETLCIGCGICIKKCPFG 68
Cdd:cd10560 76 DVCK--HCTDAgCLEACPTgaiFR--------TEFGTV-YIQPDICNGCGYCVAACPFG 123
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
205-286 |
1.58e-03 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 40.15 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 205 DLTHLKERNVeDLSGGELQRFACAVVCIQKADIFMFDEPSSYLD--VKQRLkaaitIRSLINP----DRYIIVVEHDLSV 278
Cdd:cd03250 117 DLTEIGEKGI-NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDahVGRHI-----FENCILGlllnNKTRILVTHQLQL 190
|
....*...
gi 108773782 279 LDYlSDFI 286
Cdd:cd03250 191 LPH-ADQI 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
99-276 |
1.64e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 40.55 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 99 IPRpGEVLGLVGTNGIGKSTALKILAGKQKPnlgkyDDPPD---------------W---QEILTYFRGSELQnYFTKIL 160
Cdd:PRK13640 30 IPR-GSWTALIGHNGSGKSTISKLINGLLLP-----DDNPNskitvdgitltaktvWdirEKVGIVFQNPDNQ-FVGATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 161 EDDLkaiikpqyvdqipkaAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMF 240
Cdd:PRK13640 103 GDDV---------------AFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 108773782 241 DEPSSYLDVKQRLKAAITIRSLINPDRY-IIVVEHDL 276
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLtVISITHDI 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
212-284 |
1.69e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 212 RNVEDLSGGELQRFACAVVCIQKAD---IFMFDEPSSYL---DVKQRLKaaiTIRSLINPDRYIIVVEHDLSVL---DYL 282
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLLE---VLQRLVDKGNTVVVIEHNLDVIktaDYI 901
|
..
gi 108773782 283 SD 284
Cdd:TIGR00630 902 ID 903
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
205-248 |
1.78e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 108773782 205 DLTHLKERNVeDLSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:PLN03130 730 DLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
462-537 |
1.78e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 462 LSGGELQRVALALCLGKPADVYLIDEPSAYLDSeqrlMAARVVKRFI--LHAKKTAFVVEHDFIMATYLADR-VIVFDG 537
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP----TTTEKIEEFIrsLADRLTVIIVTHNLAQAARISDRaALFFDG 238
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
21-73 |
1.89e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 38.47 E-value: 1.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 108773782 21 CRQ--ECKKSCP----------VVRMGK-------LCIEVTPQSKI----AWISETLCIGCGICIKKCPFGALSIV 73
Cdd:cd16372 49 CNQcgECIDVCPtgaitrdangVVMINKklcvgclMCVGFCPEGAMfkheDYPEPFKCIACGICVKACPTGALELV 124
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-532 |
2.03e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.21 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 374 IMVMLGENGTGKTTFIRMLAGRLKPDEG----GEVPVLNVSYKPQKISP----KSTGSVRQllhekIRDAYTHPQFVTDV 445
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFNRLLELNEEarveGEVRLFGRNIYSPDVDPievrREVGMVFQ-----YPNPFPHLTIYDNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 446 MKPLQIENI------IDQEVQ---------------------TLSGGELQRVALALCLGKPADVYLIDEPSAYLDSeqrl 498
Cdd:PRK14267 107 AIGVKLNGLvkskkeLDERVEwalkkaalwdevkdrlndypsNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP---- 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 108773782 499 MAARVVKRFILHAKK--TAFVVEHDFIMATYLADRV 532
Cdd:PRK14267 183 VGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYV 218
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
52-73 |
2.27e-03 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 36.65 E-value: 2.27e-03
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
3-73 |
2.33e-03 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 38.00 E-value: 2.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 3 DKLTRIAIVNHDKCKpkKCRQeCKKSCPvvrmgKLCIEVTPQSKIAwISETLCIGCGICIKKCPFGALSIV 73
Cdd:PRK09623 40 DWRTFMPVVDESKCV--KCYI-CWKFCP-----EPAIYIKEDGYVA-IDYDYCKGCGICANECPTKAITMV 101
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
21-75 |
2.37e-03 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 38.76 E-value: 2.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 108773782 21 CRQeCKKSCPVVrmgklCIEVTPQSKIAW---ISETLCIGCGICIKKCPFGALSIVNL 75
Cdd:cd10564 88 CRS-CQDACPTQ-----AIRFRPRLGGIAlpeLDADACTGCGACVSVCPVGAITLTPL 139
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
462-531 |
2.52e-03 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 39.72 E-value: 2.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 462 LSGGELQRVALALCL-GKPAdVYLIDEPSAYLDSEQrlmAARVVK-RFILHAKK--TAFVVEHDfimaTYLADR 531
Cdd:COG4181 147 LSGGEQQRVALARAFaTEPA-ILFADEPTGNLDAAT---GEQIIDlLFELNRERgtTLVLVTHD----PALAAR 212
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
102-281 |
2.54e-03 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 39.70 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 102 PGEVLGLVGTNGIGKSTAlkilagkqkpnlgkyddppdwqeILTYFRGSELQNYFTKILEDDLKAI----------IKPQ 171
Cdd:cd03369 33 AGEKIGIVGRTGAGKSTL-----------------------ILALFRFLEAEEGKIEIDGIDISTIpledlrssltIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 172 yvDqiPKAAKGTVGSILDRKDETKTQAIvcqqldLTHLK-ERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVK 250
Cdd:cd03369 90 --D--PTLFSGTIRSNLDPFDEYSDEEI------YGALRvSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190
....*....|....*....|....*....|..
gi 108773782 251 QRLKAAITIRSLINpDRYIIVVEHDL-SVLDY 281
Cdd:cd03369 160 TDALIQKTIREEFT-NSTILTIAHRLrTIIDY 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
205-291 |
2.57e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 41.08 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 205 DLTHLKERNVeDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV---KQRLKAAITIRSLI-NPDRyiIVVEHDLSVLD 280
Cdd:TIGR00957 750 DRTEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgKHIFEHVIGPEGVLkNKTR--ILVTHGISYLP 826
|
90
....*....|.
gi 108773782 281 YLsDFICCLYG 291
Cdd:TIGR00957 827 QV-DVIIVMSG 836
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
462-536 |
2.62e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 40.57 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 462 LSGGELQRVALALCLGKPADVYLIDEPSAYLDS--EQRLMAA--RVVKRfilhakKTAFVVEH------DfimatylADR 531
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSrtERAIQAAlrEVARG------RTTLVIAHrlstivD-------ADE 561
|
....*
gi 108773782 532 VIVFD 536
Cdd:COG5265 562 ILVLE 566
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
103-244 |
2.63e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 39.86 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 103 GEVLGLVGTNGIGKSTALKILAGKQKPNLGKyddppdwqeilTYFRGSELQNYFT-KILEDDLKAIIKPQYVdqipkAAK 181
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGDPRATSGR-----------IVFDGKDITDWQTaKIMREAVAIVPEGRRV-----FSR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 108773782 182 GTVGSILDR----KDETKTQAIVCQQLDL-THLKERNVE---DLSGGELQRFACAVVCIQKADIFMFDEPS 244
Cdd:PRK11614 95 MTVEENLAMggffAERDQFQERIKWVYELfPRLHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
84-125 |
2.73e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 40.55 E-value: 2.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 108773782 84 THRYCA----NAFKLHrlPIP---RPGEVLGLVGTNGIGKSTALKILAG 125
Cdd:COG4615 334 TYRYPGedgdEGFTLG--PIDltiRRGELVFIVGGNGSGKSTLAKLLTG 380
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
96-262 |
2.95e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 96 RLPiprPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEIltyfrgselqnyftKILEddlkaIIKPQYVDQ 175
Cdd:PRK11819 346 SLP---PGGIVGIIGPNGAGKSTLFKMITGQEQPDSG---------TI--------------KIGE-----TVKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 176 IPKA--AKGTV------GsiLDR----KDETKTQAIVC--------QQldlthlkeRNVEDLSGGELQRFACAVVCIQKA 235
Cdd:PRK11819 395 SRDAldPNKTVweeisgG--LDIikvgNREIPSRAYVGrfnfkggdQQ--------KKVGVLSGGERNRLHLAKTLKQGG 464
|
170 180
....*....|....*....|....*..
gi 108773782 236 DIFMFDEPSSYLDVKqrlkaaiTIRSL 262
Cdd:PRK11819 465 NVLLLDEPTNDLDVE-------TLRAL 484
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
457-520 |
2.97e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 2.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 457 QEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDseqrLMAARVVKRFILHAKKTAFVVEH 520
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD----LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
101-277 |
3.15e-03 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 39.52 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILagkqkPNLgkYDdpPDWQEILtyFRGSELQNYFTKiledDLKAIIKpqYVDQIPKAA 180
Cdd:cd03251 26 PAGETVALVGPSGSGKSTLVNLI-----PRF--YD--VDSGRIL--IDGHDVRDYTLA----SLRRQIG--LVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 181 KGTVG-SIL-DRKDETKTQAIVCQQLDLTH-------------LKERNVEdLSGGELQRFACAVVCIQKADIFMFDEPSS 245
Cdd:cd03251 89 NDTVAeNIAyGRPGATREEVEEAARAANAHefimelpegydtvIGERGVK-LSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190
....*....|....*....|....*....|....
gi 108773782 246 YLDV--KQRLKAAitIRSLINpDRYIIVVEHDLS 277
Cdd:cd03251 168 ALDTesERLVQAA--LERLMK-NRTTFVIAHRLS 198
|
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
50-70 |
3.19e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 35.28 E-value: 3.19e-03
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
54-74 |
3.24e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 40.36 E-value: 3.24e-03
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
47-76 |
3.28e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 39.78 E-value: 3.28e-03
10 20 30
....*....|....*....|....*....|
gi 108773782 47 IAWISETLCIGCGICIKKCPFGAlsIVNLP 76
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACPVDA--IVGAP 106
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
460-518 |
3.58e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 3.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 108773782 460 QTLSGGELQRVALALCLG----KPADVYLIDEPSAYLDSEQRLMAARVVKRfilHAKKTA-FVV 518
Cdd:cd03239 93 QILSGGEKSLSALALIFAlqeiKPSPFYVLDEIDAALDPTNRRRVSDMIKE---MAKHTSqFIV 153
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
101-262 |
3.60e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 39.69 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGK-YDDPPDWQEILTYFR-----GSELQN----YFTKILEDDLKaiIKP 170
Cdd:PRK13633 34 KKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKvYVDGLDTSDEENLWDirnkaGMVFQNpdnqIVATIVEEDVA--FGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 171 QYVDQIPKAAKGTVGSILDRKD--ETKTQAivcqqldlTHLkernvedLSGGELQRFACAVVCIQKADIFMFDEPSSYLD 248
Cdd:PRK13633 112 ENLGIPPEEIRERVDESLKKVGmyEYRRHA--------PHL-------LSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170
....*....|....
gi 108773782 249 VKQRLKAAITIRSL 262
Cdd:PRK13633 177 PSGRREVVNTIKEL 190
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
49-74 |
4.05e-03 |
|
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).
Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 39.07 E-value: 4.05e-03
10 20
....*....|....*....|....*.
gi 108773782 49 WISETlCIGCGICIKKCPFGALSIVN 74
Cdd:NF038196 182 HVTDK-CIGCGICAKVCPVNNIEMED 206
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
457-533 |
4.19e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 457 QEVQTLSGGELQRVALALCLG----KPADVYLIDEPSAYLDSEQrlmAARVVKRFILHAKKTAF-VVEHDFIMATYlADR 531
Cdd:TIGR02169 1070 QRLEAMSGGEKSLTALSFIFAiqryKPSPFYAFDEVDMFLDGVN---VERVAKLIREKAGEAQFiVVSLRSPMIEY-ADR 1145
|
..
gi 108773782 532 VI 533
Cdd:TIGR02169 1146 AI 1147
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
101-289 |
4.34e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 101 RPGEVLGLVGTNGIGKSTALKILAGKQKPNLGkyddppdwqEILtyFRGSELQNYFTK--------ILEDDLKAIIKPQY 172
Cdd:PRK10982 22 RPHSIHALMGENGAGKSTLLKCLFGIYQKDSG---------SIL--FQGKEIDFKSSKealengisMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 173 VDQIPKAAKGTVGSILDRK---DETKTqaiVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDV 249
Cdd:PRK10982 91 MDNMWLGRYPTKGMFVDQDkmyRDTKA---IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 108773782 250 KQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
450-536 |
4.40e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.38 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 450 QIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRfiLHAKKTAFVVEHDFIMATYLA 529
Cdd:PRK14243 140 EVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE--LKEQYTIIIVTHNMQQAARVS 217
|
....*..
gi 108773782 530 DRVIVFD 536
Cdd:PRK14243 218 DMTAFFN 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
211-284 |
5.02e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 211 ERNVEDLSGGELQRFACA---------VvciqkadIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHD---LSV 278
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLAtqigsgltgV-------LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDedtIRA 555
|
....*.
gi 108773782 279 LDYLSD 284
Cdd:TIGR00630 556 ADYVID 561
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
44-70 |
5.96e-03 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 37.59 E-value: 5.96e-03
10 20
....*....|....*....|....*..
gi 108773782 44 QSKIAWISETLCIGCGICIKKCPFGAL 70
Cdd:PRK08764 76 LPQVAWIVEADCIGCTKCIQACPVDAI 102
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
25-79 |
6.49e-03 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 38.82 E-value: 6.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 108773782 25 CKKSCPVVrmgklCIEVTPQsKIAWISETLCIGCGICIKKCPFGALSIVNLPSNL 79
Cdd:COG2878 145 CIKACPFD-----AIVGAAK-GMHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTV 193
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
49-91 |
6.51e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 35.30 E-value: 6.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 108773782 49 WISETLCIGCGICIKKCPFGALSIVNLPSNLEKE---------TTHRYCANA 91
Cdd:pfam13237 3 VIDPDKCIGCGRCTAACPAGLTRVGAIVERLEGEavrigvwkcIGCGACVEA 54
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
55-74 |
6.82e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 38.76 E-value: 6.82e-03
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
209-274 |
6.98e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 38.57 E-value: 6.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 108773782 209 LKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEH 274
Cdd:PRK13649 138 LFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
25-70 |
7.04e-03 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 34.84 E-value: 7.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 108773782 25 CKKSCPVVRMGKLCIEVTPQSKIAwisETLCIGCGICIKKCPFGAL 70
Cdd:pfam13187 8 CVAACPAGAIVPDLVGQTIRGDIA---GLACIGCGACVDACPRGAI 50
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
358-497 |
7.22e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 38.23 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 358 GEFELAIVAGEftdseIMVMLGENGTGKTTFIRMLAGRLKPD--EGGEVPVLNVSYKPQKISPKSTG------------S 423
Cdd:COG4136 18 APLSLTVAPGE-----ILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNGRRLTALPAEQRRIGilfqddllfphlS 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 108773782 424 VRQLLHEKIRDAYTHPQFVTDVMKPLQ---IENIIDQEVQTLSGGELQRVAL--ALcLGKPAdVYLIDEPSAYLDSEQR 497
Cdd:COG4136 93 VGENLAFALPPTIGRAQRRARVEQALEeagLAGFADRDPATLSGGQRARVALlrAL-LAEPR-ALLLDEPFSKLDAALR 169
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
450-552 |
7.59e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 38.49 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 108773782 450 QIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDseqrLMAARVVKRFILHAKK--TAFVVEHDFIMATY 527
Cdd:PRK14246 142 EVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID----IVNSQAIEKLITELKNeiAIVIVSHNPQQVAR 217
|
90 100 110
....*....|....*....|....*....|
gi 108773782 528 LADRV-IVFDG----VPSKNTVANSPQTLL 552
Cdd:PRK14246 218 VADYVaFLYNGelveWGSSNEIFTSPKNEL 247
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
107-132 |
8.16e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 8.16e-03
10 20
....*....|....*....|....*.
gi 108773782 107 GLVGTNGIGKSTALKILAGKQKPNLG 132
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAG 56
|
|
| |
